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276 results for “protein domains”
SIRAH-CoV2 initiative: Nucleocapsid protein N-terminal RNA binding domain (PDB id:6M3M)
<p>This dataset contains the trajectory of a 10 microseconds-long coarse-grained molecular dynamics simulation of SARS-CoV2 Nucleocapsid protein N-terminal RNA binding domain (PDB id:6M3M). Simulations have been performed using the SIRAH force field running with the Amber18 package at the Uruguayan National Center for Supercomputing (ClusterUY) under the conditions reported in <a href="https://pubs.acs.org/doi/10.1021/acs.jctc.9b00006">Machado et al. JCTC 2019</a>, adding 150 mM NaCl according to <a href="https://pubs.acs.org/doi/10.1021/acs.jctc.9b00953">Machado & Pantano JCTC 2020</a>. </p> <p>The files 6M3M_SIRAHcg_rawdata.tar contains all the raw information required to visualize (on VMD), analyze, backmap, and eventually continue the simulations using Amber18 or higher. Step-By-Step tutorials for running, visualizing, and analyzing CG trajectories using <a href="https://academic.oup.com/bioinformatics/article/32/10/1568/1743152">SirahTools</a> can be found at www.sirahff.com.</p> <p>Additionally, the file 6M3M_SIRAHcg_10us_prot.tar contains only the protein coordinates, while 6M3M_SIRAHcg_10us_prot_skip10ns.tar contains one frame every 10ns.</p> <p>To take a quick look at the trajectory:</p> <p>1- Untar the file 6M3M_SIRAHcg_10us_prot_skip10ns.tar</p> <p>2- Open the trajectory on VMD using the command line:</p> <p>vmd 6W4B_SIRAHcg_prot.prmtop 6W4B_SIRAHcg_prot.ncrst 6W4B_SIRAHcg_prot_10us_skip10ns.nc -e sirah_vmdtk.tcl</p> <p>Note that you can use normal VMD drawing methods as vdw, licorice, etc., and coloring by restype, element, name, etc. </p> <p>This dataset is part of the SIRAH-CoV2 initiative.</p> <p>For further details, please contact Florencia Klein (fklein@pasteur.edu.uy) or Sergio Pantano (spantano@pasteur.edu.uy).</p>
Human Pleckstrin Homology domain Interacting Protein (PHIP); A Target Enabling Package
<p>SGC Oxford has expressed, purified and crystallized the second bromodomain of PHIP as part of the probe programme. Fragment screening and X-ray crystallography identified binders, some of which optimised to uM affinity. However, molecules with probe properties were not obtained. Consequently it has been decided to put the information generated into the public domain.</p>
Dehydrogenase E1 and transketolase domain-containing protein 1 (DHTKD1); A Target Enabling Package
<p>Inherited mutations of the <em>GCDH </em>gene for glutaryl-CoA dehydrogenase, catalysing the sixth enzymatic step in lysine catabolism, lead to the rare neurometabolic disorder Glutaric Aciduria type 1 (GA1). There is a rationale that inhibition of the fifth lysine catabolising step, catalysed by the DHTKD1 enzyme, could provide therapeutic benefit for GA1 by means of substrate reduction. This TEP provides early tools to develop DHTKD1 inhibitors, including recombinant protein, structure, biophysical (activity and stability) assays and fragment hits of human DHTKD1. This work also reports the interaction of DHTKD1 with its functional partner DLST as a binary complex, and an EM reconstruction of the DLST catalytic core.</p>
Dataset for: Pre-pandemic artificial MERS analog of polyfunctional SARS-CoV-2 S1/S2 furin cleavage site domain is unique among spike proteins of genus Betacoronavirus
<table> <tbody> <tr> <th> </th> <td> <div> <h3><strong>Data File Descriptions and Methods</strong></h3> <ol> <li><strong>Data file 1 [betacov_matching_IPR042578.fasta]</strong>: Representative set of 2,465 betacoronavirus S protein overlapping homologous superfamily sequences retrieved in fasta format on 4 December 2022 from the InterPro repository at https://www.ebi.ac.uk/interpro/entry/InterPro/IPR042578/.<br><br></li> <li><strong>Data File 2 [betacov_matching_IPR042578_motif.fasta]</strong>: With Data File 1 as input, extracted 98,122 furin cleavage site (FCS) output motifs of 20 amino acids length, including overlapping and redundant sequences, produced with the FindFur algorithm with preset parameters as described by (Gu, 2020). FindFur as used was deposited on 15 December 2020 at the GitHub software repository at https://github.com/chwisteeng/FindFur.<br><br></li> <li><strong>Data File 3 [table_s1s2_hits_betacov_polyf.pdf]</strong>: Compiled summary table of sequence hits (PDF) of spike S1/S2 domains across genus <em>Betacoronavirus. </em>The compiled table of hits removed from Data File 2 sequences corresponding to spike protein fragments (incomplete length spike proteins as deposited at GenBank) and duplicates (redundant parts identically overlapping within the 20 amino acids motif windows), and then selected one sequence representative for multiple but identical sequences.<em> </em>Collection dates and geographical locations were retrieved from the NCBI Genbank protein database at https://www.ncbi.nlm.nih.gov/protein/. For SARS-CoV-2 spike variants, these data were also cross-validated with the SARS-CoV-2 lineage mutation tracker (Gangavarapu, 2023) available at https://outbreak.info which was based on extensive sequencing data from the global GISAID initiative (https://gisaid.org/). Solid lines (-) depict pat7 NLS, asterisks (*) O-glycosites, and circumflex (^) symbols FCS.<br><br></li> <li> <p><strong>Data File 4 [table_s1s2_hits_betacov_polyf.xlsx]</strong>: Compiled summary table of sequence hits (MS Excel) of spike S1/S2 domains across genus <em>Betacoronavirus. </em>The compiled table of hits removed from Data File 2 sequences corresponding to spike protein fragments (incomplete length spike proteins as deposited at GenBank) and duplicates (redundant parts identically overlapping within the 20 amino acids motif windows), and then selected one sequence representative for multiple but identical sequences.<em> </em>Collection dates and geographical locations were retrieved from the NCBI Genbank protein database at https://www.ncbi.nlm.nih.gov/protein/. For SARS-CoV-2 spike variants, these data were also cross-validated with the SARS-CoV-2 lineage mutation tracker (Gangavarapu, 2023) available at https://outbreak.info which was based on extensive sequencing data from the global GISAID initiative (https://gisaid.org/). Solid lines (-) depict pat7 NLS, asterisks (*) O-glycosites, and circumflex (^) symbols FCS.<br><br></p> </li> <li> <p><strong>Data File 5 [betacov_s1s2_nls_pat7_furin_psort.txt]: </strong>Nuclear localization signal (NLS) detection output for 5 representative betacoronavirus spike sequence domains, including the positive hits for pat7 in SARS-CoV-2 and for MERS-MA30 CoV. NLS predictions used the PSORT algorithm available as a webservice at https://wolfpsort.hgc.jp/ which is based on the work of Nakai and Horton (Nakai and Horton, 1999). Numbering refers to Data File 3 and Data File 4.<br><br></p> </li> <li> <p><strong>Data File 6 [betacov_s1s2_oglyc_netogly.txt]: </strong>Detection output for 5 representative betacoronavirus spike sequence domains tested for Thr/Ser O-glycosite residue pairs with the standard prediction software NetOGlyc4.0 (Steentoft et al., 2013) as available at https://services.healthtech.dtu.dk/services/NetOGlyc-4.0/. Positive hits have scores above 0.5. Numbering refers to Data File 3 and Data File 4.<br><br></p> </li> <li> <p><strong>Data File 7 [betacov_s1s2_nls_pat7_furin_blastp.txt]</strong>: Comprehensive sequence database searches using were performed using the NCBI protein BLAST (blastp) algorithm with webservice available at https://blast.ncbi.nlm.nih.gov/Blast.cgi?PAGE=Proteins. The following blastp search parameters and settings were used: Word size=2; Expect value=200000; Hitlist size=500; Gapcosts=9,1; Matrix=PAM30; Filter string=F; Genetic Code=1;Window Size=40; Threshold=11; Composition-based stats=0; Database Posted date=Jan 19, 2023 2:59 AM; Number of letters=17,117,563; Number of sequences=10,766; Entrez query: Includes: Betacoronavirus (taxid:694002); Excludes: SARS-CoV-2 (taxid:2697049). The six polyfunctional input query consensus motif sequences were TXXPR(K/H/R)XRSX and TXXPRX(K/H/R)RSX.</p> </li> </ol> <h3><strong>References</strong></h3> <p>Gu, C., 2020. FindFur: A Tool for Predicting Furin Cleavage Sites of Viral Envelope Substrates. Master’s Thesis, San Jose State University, CA, USA. doi: <a href="https://doi.org/10.31979/etd.4ahv-9jya">10.31979/etd.4ahv-9jya</a> </p> <p>Gangavarapu K, Latif AA, Mullen JL, Alkuzweny M, Hufbauer E, Tsueng G, Haag E, Zeller M, Aceves CM, Zaiets K, Cano M, Zhou X, Qian Z, Sattler R, Matteson NL, Levy JI, Lee RTC, Freitas L, Maurer-Stroh S; GISAID Core and Curation Team; Suchard MA, Wu C, Su AI, Andersen KG, Hughes LD. Outbreak.info genomic reports: scalable and dynamic surveillance of SARS-CoV-2 variants and mutations. Nat Methods. 2023. 20(4):512-522. doi: <a href="https://doi.org/10.1038/s41592-023-01769-3">10.1038/s41592-023-01769-3</a>.</p> <p>Nakai, K., Horton, P., 1999. PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem Sci 24, 34–36. doi: <a href="https://doi.org/10.1016/s0968-0004(98)01336-x">10.1016/s0968-0004(98)01336-x</a></p> <p>Steentoft, C., Vakhrushev, S.Y., Joshi, H.J., Kong, Y., Vester-Christensen, M.B., Schjoldager, K.T.-B.G., Lavrsen, K., Dabelsteen, S., Pedersen, N.B., Marcos-Silva, L., Gupta, R., Bennett, E.P., Mandel, U., Brunak, S., Wandall, H.H., Levery, S.B., Clausen, H., 2013. Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology. EMBO J 32, 1478–1488. doi: <a href="https://doi.org/10.1038/emboj.2013.79">10.1038/emboj.2013.79</a></p> </div> </td> </tr> </tbody> </table>
Major facilitator superfamily domain-containing protein 10 (MFSD10) A Target Enabling Package (TEP)
<p>MFSD10 (also known as TETRAN in humans) has been proposed to function as an organic anion efflux pump and as a transporter for some NSAIDs. We have produced milligram quantities of purified recombinant protein and solved its structure in an outward-facing state at 2.6 Å resolution by X-ray crystallography. The structure - the first example for a human atypical SLC - provides the initial clues to understanding the broad specificity of its putative substrate-binding site.</p>
Supplementary data files for exploring a diverse world of effector domains and amyloid signaling motifs in fungal NLR proteins
<p>This dataset includes 20 supplementary data files for manuscript <em>Exploring a diverse world of effector domains and amyloid signaling motifs in fungal NLR proteins </em>by Jakub W. Wojciechowski, Emirhan Tekoglu, Marlena Gąsior-Głogowska, Virginie Coustou, Natalia Szulc, Monika Szefczyk, Marta Kopaczyńska, Sven J. Saupe, and Witold Dyrka (under revision). </p> <ul> <li>SF2. Profile HMMs of NLR effector domains. The file includes previously unpublished models.</li> <li>SF3. Multiple sequence alignments of N-termini clusters. </li> <li>SF4. Tabularized results of N-termini annotation.</li> <li>SF5. Structure prediction of HeLo-/Goodbye-/MLKL-like domains. Full AlphaFold2/ColabFold outputs.</li> <li>SF6. Structure prediction of previously unannotated domains. Full AlphaFold2/ColabFold outputs.</li> <li>SF7. PCFGs for BASS. The file includes previously unpublished grammars and a sample scanning configuration.</li> <li>SF8. Candidate short NLR N-termini with ASMs. The FASTA file includes sequences from clusters with high content of ASM-like sequences, according to the BASS PCFGs (SF7).</li> <li>SF9. Profile HMMs of ASMs found in short NLR N-termini.</li> <li>SF10. Profile HMM of HeLo-related HRAMs.</li> <li>SF11. Genomic neighbors of candidate short N-termini NLRs with ASMs The list includes accessions of proteins encoded by genes within the neighborhood of 20kbp of genes encoding the query proteins (SF8).</li> <li>SF12. Short C-termini of 200–400 aa long proteins genomically neighboring candidate short NLR N-termini with ASMs. The FASTA file concerns target proteins listed in SF11.</li> <li>SF13. Pairwise hits of the same ASMs in N-termini of NLRs and C-termini of genomically neighboring proteins. The table is based on SF8–9 and SF11–12. </li> <li>SF14. Lists of HMMER domain hits of effector domain profiles. The lists were obtained through iterative searches in NCBI “nr” starting from Pfam profiles of known NLR effector domains.</li> <li>SF15. Short C-termini of effector proteins. The FASTA file concerns target proteins listed in SF14.</li> <li>SF16. Short N-termini of Pfam NACHT and NB-ARC proteins. The FASTA file concerns proteins from NCBI “nr” associated with the two families in the Pfam database.</li> <li>SF17. Profile HMMs of ASMs found both in effector C-termini and NLR N-termini of genomically neighboring proteins.</li> <li>SF18. Genomic neighbors of candidate short N-termini Pfam NACHT and NB-ARC proteins. The list includes accessions of proteins encoded by genes within the neighborhood of 20kbp of genes encoding the query proteins (SF16).</li> <li>SF19. Pairwise hits of the same ASMs in N-termini of NACHT/NB-ARC NLRs and C-termini of genomically neighboring effector proteins. The table is based on SF15–18. </li> <li>SF20. Pairwise hits of the same ASMs in N-termini of NLRs and C-termini of genomically co-occurring effector proteins. The table is based on SF8–9 and SF15. </li> <li>SF21. BaMLKL homologs identified with hmmsearch in Basidiomycota. A FASTA file.</li> </ul>
Mapping of protein domains to exons
<p>Database table maps transcripts and exons to their isoforms and Pfam domains. </p> <p>Originally generated from Ensembl Biomart </p> <p>If you use the database, please cite:</p> <p>Zakaria Louadi, Kevin Yuan, Alexander Gress, Olga Tsoy, Olga V Kalinina, Jan Baumbach, Tim Kacprowski*, Markus List*. <a href="https://doi.org/10.1093/nar/gkaa768">DIGGER: exploring the functional role of alternative splicing in protein interactions</a>, Nucleic Acids Research.<br> * Joint last authors.</p> <p>Source code of DIGGER: <a href="https://github.com/louadi/DIGGER">https://github.com/louadi/DIGGER</a></p>
Heatmaps of orthology and protein domain preservation in RNA Processing complexes throughout the fungal kingdom
<p>An analysis of the presence/absence of orthologues for Fungal RNA Processing protein complexes, and the presence/absence of the known PFAM protein domains within each protein within these complexes in the organism's proteome. </p> <p>Each image represents one RNA Processing protein complex.</p> <p>Orthology (far left panel in each image) is relative to Yeast, and taken from a query against the EnsEMBL orthology database (black = no orthologue; red = orthologue). <br> <br> Each orthologue was then queried for its PFAM domains, and the non-redundant set of PFAM domains representing each set of orthologous proteins, spanning all species, was then scanned against the complete proteome of each species. The resulting heatmap indicates the presence or absence of that PFAM domain anywhere in the proteome of that species. (black = absent; red = 1 copy; grey->blue = more than one copy)</p>
Predictions of the SARS-CoV-2 B.1.1.529 Variant Spike Protein Receptor Binding Domain Structure and Neutralizing Antibody Interactions
<p>Using AlphaFold2 and HADDOCK, we have generated a predicted structure for the SARS-CoV-2 B.1.1.529 variant's Spike receptor binding domain and then predicted the binding interaction with neutralizing antibodies. This was performed to understand the potential structural changes in the receptor binding domain of B.1.1.529 and how this may affect vaccine efficacy through antibody interaction.</p>
Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (Proline-serine-threonine phosphatase-interacting protein 1) mutant G258A (PDB entry 7AAL)
<p>Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (residues 1-289), mutant G258A.</p> <p>Data were collected on a single crystal at the beamline i03 of the Diamond Light Source synchrotron (Didcot, UK) using radiation of 0.9999 Å wavelength and a PILATUS3 6M detector. The dataset consists of 2400 images (0.15 degree oscillation per image). Crystals belong to the space group P2(1)2(1)2(1) with unit cell dimensions a=48.19 Å, b=73.02 Å, c=205.25 Å. The asymmetric unit contains an homodimer of the F-BAR domain (~53% solvent content), which is the biological unit.</p> <p>Diffraction data was notably anisotropic. The lowest resolution limit was 2.92 Å in the direction b* and the highest limits were 1.97 Å and 2.09 in the directions a* and c*, respectively.</p> <p> </p> <p>The structure derived form these data is published in:</p> <p>Manso, J.A., Marcos, T., Ruiz-Martín, V. Casas J, Alcón P, Sánchez Crespo M, Bayón Y, de Pereda JM, Alonso A <em>PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders</em>. <strong>Cell. Mol. Life Sci</strong>. 79, 131 (2022). <a href="https://doi.org/10.1007/s00018-022-04173-w">https://doi.org/10.1007/s00018-022-04173-w</a></p> <p>The structure is available at the PDB under the code 7AAL:</p> <p><a href="https://www.ebi.ac.uk/pdbe/entry/pdb/7aal">https://www.ebi.ac.uk/pdbe/entry/pdb/7aal</a></p>
Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (Proline-serine-threonine phosphatase-interacting protein 1) bound to the C-terminal homology (CTH) segment of the phosphatase LYP (PTPN22) (PDB entry 7AAM)
<p>Diffraction images of a crystal of the F-BAR domain of human PSTPIP1 (residues 1-289, Uniprot reference O43586-1) in complex with the CTH of LYP (residues 787-807, Uniprot Q9Y2R2-1).</p> <p>Data were collected on a single crystal at the beamline i03 of the Diamond Light Source synchrotron (Didcot, UK) using radiation of 0.99987 Å wavelength and a PILATUS3 6M detector. The dataset consists of 3 groups, each containing of 1800 images (0.1 degree oscillation per image), collected at three different positions of the same crystal. Crystal belongs to the space group P2(1)2(1)2(1) with unit cell dimensions a=48.0 Å, b=72.0 Å, c=205.0 Å. The asymmetric unit contains an homodimer of the F-BAR domain bound to a LYP-CTH (~53% solvent content), which is the biological complex.</p> <p>Diffraction data was notably anisotropic. The lowest resolution limit was 4.05 Å in the direction b* and the highest limits were 2.11 Å and 2.10 in the directions a* and c*, respectively.</p> <p> </p> <p>The structure derived form these data is published in:</p> <p>Manso, J.A., Marcos, T., Ruiz-Martín, V. Casas J, Alcón P, Sánchez Crespo M, Bayón Y, de Pereda JM, Alonso A <em>PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders</em>. <strong>Cell. Mol. Life Sci</strong>. 79, 131 (2022). <a href="https://doi.org/10.1007/s00018-022-04173-w">https://doi.org/10.1007/s00018-022-04173-w</a></p> <p>The structure is available at the PDB under the code <strong>7AAM</strong>:</p> <p><a href="https://www.ebi.ac.uk/pdbe/entry/pdb/7aam">https://www.ebi.ac.uk/pdbe/entry/pdb/7aam</a></p>
Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (Proline-serine-threonine phosphatase-interacting protein 1) (PDB entry 7AAN)
<p>Diffraction images of a crystal of the F-BAR domain of PSTPIP1 (residues 1-289).</p> <p>Data were collected on a single crystal at the beamline i03 of the Diamond Light Source synchrotron (Didcot, UK) using radiation of 0.99987 Å wavelength and a PILATUS3 6M detector. The dataset consists of 3600 images (0.15 degree oscillation per image) that were collected: 2400 at one position and the other 1200 at a second site in the same crystal. Crystal belongs to the space group P2(1)2(1)2(1) with unit cell dimensions a=48.3 Å, b=71.9 Å, c=204.6 Å. The asymmetric unit contains an homodimer of the F-BAR domain (~53% solvent content), which is the biological unit.</p> <p>Diffraction data was notably anisotropic. The lowest resolution limit was 4.32 Å in the direction b* and the highest limits were 2.12 Å and 2.17 in the directions a* and c*, respectively.</p> <p>The structure derived form these data is published in:</p> <p>Manso, J.A., Marcos, T., Ruiz-Martín, V. Casas J, Alcón P, Sánchez Crespo M, Bayón Y, de Pereda JM, Alonso A <em>PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders</em>. <strong>Cell. Mol. Life Sci</strong>. 79, 131 (2022). <a href="https://doi.org/10.1007/s00018-022-04173-w">https://doi.org/10.1007/s00018-022-04173-w</a></p> <p>The structure is available at the PDB under the code <strong>7AAN</strong>:</p> <p><a href="https://www.ebi.ac.uk/pdbe/entry/pdb/7aan">https://www.ebi.ac.uk/pdbe/entry/pdb/7aan</a></p>
MD simulation of the crystal unit cell of the second PDZ domain of LNX2 protein
<p>This molecular dynamics simulation data is provided as part of the manuscript "<strong>LAWS: Local Alignment for Water Sites - a method to analyze crystallographic water in simulations</strong>". The code for the algorithm is provided: <a href="https://github.com/rauscher-lab/LAWS">on github</a><br> <br> The system contains one unit cell of the crystal (PDB ID: 5E11) with 4 symmetrically related protein chains. The total simulation length is 1 microsecond. </p> <p><strong>Force field + water model</strong>: CHARMM36m + CHARMM-modified TIP3P<br> <strong>Number of atoms</strong>: 9650<br> <strong>Number of time frames:</strong> 100,000 with 10-ps stride<br> <em>The details of the simulations are provided in the manuscript.</em></p>
Simulation of Receptor Binding Domain of SARS-CoV-2 spike protein (WT and variants) in complex with neutralizing antibodies.
<p>This repository contains the molecular dynamics trajectories of the SARS-CoV-2 Spike RBD bound to BD23 and B38 monoclonal antibodies. The simulations for the RBD only systems are also provided. The trajectories are available for the WT spike protein as well as for four different variants (alpha, beta, kappa and delta). The simulations of the RBD only system are propagated for 300 ns and for the RBD-Antibody complex for 500 ns. The trajectories are saved at 100 ps interval. The Steered MD simulation trajectories (WT_RBD_B38_SMD_1.dcd etc.) and collective variables files are also included (WT_RBD_B38_SMD_1.colvars.traj etc.). There are 5 SMD trajectories for each RBD antibody pair. The details of the simulation can be obtained from the preprint: https://doi.org/10.1101/2021.08.13.456317</p>
A structural database of chain-chain and domain-domain interfaces of proteins
<p>Library of protein-protein and domain-domain interfaces from the protein data bank. The data also contains the structural clusters of protein-protein and domain-domain interfaces.</p>
Рис. 5. Варианты преΑсказанной Αоменной структуры скавенΑжер-рецепторов гемоцитов моΛΛюсков Planorbarius corneus. Сокращения (зΑесь и ΑаΛее): SR — богатый цистеином Αомен скавенΑжер-рецептора, Filament — Αомен промежуточного фиΛамента, TSP1 — повторы тромбоспонΑина типа 1, KR — крингΛ-Αомен, LDLa — Αомен рецептора Λипопротеинов низкой пΛотности кΛасса А Fig. 5. Variants of the predicted domain structure of scavenger receptors from hemocytes of Planorbarius corneus molluscs. Abbreviations (here and in what follows): SR — scavenger receptor Cys-rich domain, Filament — intermediate filament protein, TSP1 — thrombospondin type 1 repeats, KR — kringle domain, LDLa — low-density lipoprotein receptor domain class A in Pathogen recognition molecules from hemocytes of Planorbarius corneus molluscs (Planorbidae, Pulmonata)
Рис. 5. Варианты преΑсказанной Αоменной структуры скавенΑжер-рецепторов гемоцитов моΛΛюсков Planorbarius corneus. Сокращения (зΑесь и ΑаΛее): SR — богатый цистеином Αомен скавенΑжер-рецептора, Filament — Αомен промежуточного фиΛамента, TSP1 — повторы тромбоспонΑина типа 1, KR — крингΛ-Αомен, LDLa — Αомен рецептора Λипопротеинов низкой пΛотности кΛасса А Fig. 5. Variants of the predicted domain structure of scavenger receptors from hemocytes of Planorbarius corneus molluscs. Abbreviations (here and in what follows): SR — scavenger receptor Cys-rich domain, Filament — intermediate filament protein, TSP1 — thrombospondin type 1 repeats, KR — kringle domain, LDLa — low-density lipoprotein receptor domain class A
Рис. 2. Варианты преΑсказанной Αоменной структуры патогенраспознающих моΛекуΛ гемоцитов моΛΛюсков Planorbarius corneus. a — фибриногенпоΑобные беΛки, b — гаΛектины, c — F-Λектины. УсΛовные обозначения и сокращения, зΑесь и ΑаΛее: горизонтаΛьные красные поΛоски — сигнаΛьный пептиΑ, горизонтаΛьные розовые — обΛасть низкой сΛожности, вертикаΛьные синие поΛоски — трансмембранная обΛасть, FBG — фибриногеновый Αомен, FTP — Αомен фукоΛектина, EGF — Αомен эпиΑермаΛьного фактора роста, EGF_CA — каΛьцийсвязывающий EGF-поΑобный Αомен, PAN_AP — APPLE-поΑобный Αомен, SCAN — обΛасть, богатая Λейцином, GLECT — гаΛактозосвязывающий Λектин, CLECT — Λектин C-типа, Gal-bind — гаΛактозиΑ–связывающий Λектин, ML — MD-2- поΑробный Αомен распознавания ΛипиΑов Fig. 2. Variants of the predicted domain structure of pattern recognition molecules from hemocytes of Planorbarius corneus molluscs. a — fibrinogen-related proteins, b — galectins, c — F-lectins. Symbols and abbreviations (here and further): horizontal red stripes — signal peptide, horizontal pink stripes — a low complexity region, vertical blue stripes — transmembrane region, FBG — fibrinogen-related domain, FTP — fucolectin domain, EGF — epidermal growth factor-like domain, EGF_CA — calcium-binding EGF-like domain, PAN_AP — APPLE-like domain, SCAN — leucine rich region, Apple — APPLE domain, GLECT — galactose-binding lectin, CLECT — C-type lectin, Gal-bind — galactoside-binding lectin, ML — MD-2-related lipid-recognition domain in Pathogen recognition molecules from hemocytes of Planorbarius corneus molluscs (Planorbidae, Pulmonata)
Рис. 2. Варианты преΑсказанной Αоменной структуры патогенраспознающих моΛекуΛ гемоцитов моΛΛюсков Planorbarius corneus. a — фибриногенпоΑобные беΛки, b — гаΛектины, c — F-Λектины. УсΛовные обозначения и сокращения, зΑесь и ΑаΛее: горизонтаΛьные красные поΛоски — сигнаΛьный пептиΑ, горизонтаΛьные розовые — обΛасть низкой сΛожности, вертикаΛьные синие поΛоски — трансмембранная обΛасть, FBG — фибриногеновый Αомен, FTP — Αомен фукоΛектина, EGF — Αомен эпиΑермаΛьного фактора роста, EGF_CA — каΛьцийсвязывающий EGF-поΑобный Αомен, PAN_AP — APPLE-поΑобный Αомен, SCAN — обΛасть, богатая Λейцином, GLECT — гаΛактозосвязывающий Λектин, CLECT — Λектин C-типа, Gal-bind — гаΛактозиΑ–связывающий Λектин, ML — MD-2- поΑробный Αомен распознавания ΛипиΑов Fig. 2. Variants of the predicted domain structure of pattern recognition molecules from hemocytes of Planorbarius corneus molluscs. a — fibrinogen-related proteins, b — galectins, c — F-lectins. Symbols and abbreviations (here and further): horizontal red stripes — signal peptide, horizontal pink stripes — a low complexity region, vertical blue stripes — transmembrane region, FBG — fibrinogen-related domain, FTP — fucolectin domain, EGF — epidermal growth factor-like domain, EGF_CA — calcium-binding EGF-like domain, PAN_AP — APPLE-like domain, SCAN — leucine rich region, Apple — APPLE domain, GLECT — galactose-binding lectin, CLECT — C-type lectin, Gal-bind — galactoside-binding lectin, ML — MD-2-related lipid-recognition domain
Рис. 7. Варианты преΑсказанной Αоменной структуры моΛекуΛ аΑгезии гемоцитов моΛΛюсков Planorbarius corneus. УсΛовные обозначения и сокращения: 1–3 — β-интегрины, 4–5 — α-интегрины, 6–7 — сеΛектины, 8–11 — моΛекуΛы семейства САМ (сell adhesiom molecues), INB — субъеΑиницы β-интегрина, IntegrinBcyt — цитопΛазматический Αомен β-интегрина, CY — цистатинопоΑобный Αомен, Int alpha — Αомен α-интегрина, FN3 — Αомен фибронектина типа 3, CCP — Αомен контроΛя компΛемента Fig. 7. Variants of the predicted domain structure of adhesion molecules from hemocytes of Planorbarius corneus molluscs. Symbols and abbreviations: 1–3 — β-integrins, 4–5 — α–integrins, 6–7 — selectins, 8–11 — molecules of the СAM family (cell adhesion molecules), INB — β-integrin subunits, IntegrinBcyt — cytoplasmic domain of β-integrin, CY — cystatin-like domain, Int alpha — α-integrin domain, FN3 — fibronectin type 3 domain, CCP — complement control protein domain in Pathogen recognition molecules from hemocytes of Planorbarius corneus molluscs (Planorbidae, Pulmonata)
Рис. 7. Варианты преΑсказанной Αоменной структуры моΛекуΛ аΑгезии гемоцитов моΛΛюсков Planorbarius corneus. УсΛовные обозначения и сокращения: 1–3 — β-интегрины, 4–5 — α-интегрины, 6–7 — сеΛектины, 8–11 — моΛекуΛы семейства САМ (сell adhesiom molecues), INB — субъеΑиницы β-интегрина, IntegrinBcyt — цитопΛазматический Αомен β-интегрина, CY — цистатинопоΑобный Αомен, Int alpha — Αомен α-интегрина, FN3 — Αомен фибронектина типа 3, CCP — Αомен контроΛя компΛемента Fig. 7. Variants of the predicted domain structure of adhesion molecules from hemocytes of Planorbarius corneus molluscs. Symbols and abbreviations: 1–3 — β-integrins, 4–5 — α–integrins, 6–7 — selectins, 8–11 — molecules of the СAM family (cell adhesion molecules), INB — β-integrin subunits, IntegrinBcyt — cytoplasmic domain of β-integrin, CY — cystatin-like domain, Int alpha — α-integrin domain, FN3 — fibronectin type 3 domain, CCP — complement control protein domain
Pleckstrin Homology domain Interacting Protein (PHIP); A Target Enabling Package
<p>SGC Oxford has expressed, purified and crystallized the second bromodomain of PHIP as part of the probe programme. Fragment screening and X-ray crystallography identified binders, some of which optimised to uM affinity. However, molecules with probe properties were not obtained. Consequently it has been decided to put the information generated into the public domain.</p>
Figure 2 in Solution structure of the first RRM domain of human spliceosomal protein SF3b49
Figure 2. – Fresh specimen of Lutjanus madras (UPVMI 1084, 211.3 mm SL, Panay Island, Republic of the Philippines).
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Allen Brain Atlas
Allen Brain Atlas is an Allen Institute collection of brain map atlases, datasets, APIs, and analysis tools covering mouse, human, and non-human primate brain resources.
Annotated Behaviour and Observability Dataset (ABODe)
ABODe is a University of Edinburgh DataShare dataset for behavior classification in group-housed mice using home-cage video, identities, bounding boxes, ground-plate positions, and annotator labels.
DANDI Archive for NWB datasets
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The International Brain Laboratory public data releases expose standardized mouse decision-making experiments, including Neuropixels recordings, widefield calcium imaging, behavior, and session metadata accessed through the ONE API.
OpenNeuro
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