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13 results for “allosteric proteins”

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zenodo44/100

Intermolecular interactions in G protein-coupled receptor allosteric sites at the membrane interface from molecular dynamics simulations and quantum chemical calculations

<p>Allosteric modulators are called to be promising candidates in G protein-coupled receptor (GPCR) drug development by displaying target selectivity and fewer side effects. Among the allosteric sites known to date, extrahelical cavities represent an uncharacteristic binding location that raises many questions about the ligand interactions and stability; the binding site structure, and how all of these are affected by lipid molecules. In this work, we analyze the dynamics and interactions in the PAR2, C5aR1, and GCGR receptors unbound and bound to allosteric modulators at the receptor-lipid interface using molecular dynamics simulations in three lipid compositions. In addition, we performed quantum chemical calculations to further explore electrostatic interactions and the strength of atom pairwise contacts in the stabilization of the ligand-receptor complexes. We show that besides classical hydrogen bonds weak polar interactions such as O-HC, O-Br, and S-HC contacts and aromatic interactions contribute to the binding of allosteric modulators at the extrahelical sites in the middle of the membrane. The allosteric cavities are open and detectable in various membrane compositions but not always predicted as druggable. &nbsp;The availability of polar atoms for interactions in such cavities can be assessed by water molecules from the simulations. Although ligand-lipid interactions are weak, the lipid tails play a role in sizing and shaping the large part of the allosteric cavity.&nbsp;</p> <p>You will find the following files:</p> <ul> <li>Input files of the equilibration and production protocols of MD simulations (MD_simulations_inputs.zip)</li> <li>Input files and coordinate files of F-SAPT and NCIPLOT calculations (quantum_chemical_coordiates_inputs.zip)</li> </ul>

opencc-by-4.0Jun 2022View details →
zenodo40/100

Neural relational inference to learn long-range allosteric interactions in proteins from molecular dynamics simulations

<p>MD simulations used in&nbsp;the studies of the publication&nbsp;&quot;<strong>Neural relational inference to learn long-range allosteric interactions in proteins from molecular dynamics simulations</strong>&quot;</p>

opencc-by-4.0Jan 2022View details →
zenodo40/100

Supplementary data and code to "Known allosteric proteins have central roles in genetic disease" by G. Abrusan, D. Ascher and M. Inouye, PLOS Computational Biology 18(2):e1009806.

<p>Scripts and data to reproduce the figures and supplementary figures of &quot;G. Abrusan, D. Ascher and M. Inouye (2022) Known allosteric proteins have central roles in genetic disease.&quot; PLOS Computational Biology 18(2):e1009806. https://doi.org/10.1371/journal.pcbi.1009806.</p>

opencc-by-4.0Mar 2023View details →
zenodo36/100

Data from: Protein Conformational Space at the Edge of Allostery: Turning a Non-allosteric Malate Dehydrogenase into an "Allosterized" Enzyme using Evolution Guided Punctual Mutations

<p>This data&nbsp;accompanies the paper&nbsp;entitled <em>Protein Conformational Space at the Edge of Allostery: Turning a Non-allosteric Malate Dehydrogenase into an &ldquo;Allosterized&rdquo; Enzyme using Evolution Guided Punctual Mutations</em></p> <p>The zip archive contains the results of molecular dynamics simulations of the 4 systems investigated in the paper: wt of A. ful MalDH and three mutants. Each system has been simulated at two temperatures, 300 K and 340 K. Starting configurations of the proteins after equilibration are provided for all the systems in GRO Gromos87 format. Trajectories with the positions of the proteins every 100 ps are provided for all the systems in XTC gromacs format.</p>

opencc-by-4.0Mar 2022View details →
zenodo36/100

Raw NGS Data for "Deep mutational scanning and machine learning reveal structural and molecular rules governing allosteric hotspots in homologous proteins"

<p>This directory contains relevant fastq files used for deep sequencing analysis in the publication &ldquo;Deep mutational scanning and machine learning reveal structural and molecular rules governing allosteric hotspots in homologous proteins&rdquo;.&nbsp;</p> <p>Fastq files are provided for presorted, uninduced and induced populations from DMS experiments of&nbsp;four&nbsp;homologs (TtgR, TetR, RolR, and MphR). Three replicates were performed for each sample.</p> <p>Data analysis of this&nbsp;deep sequencing data was performed using custom scripts, which are described in the methods section of the publication.</p>

opencc-by-4.0Aug 2022View details →
zenodo32/100

The pocketome of G-protein-coupled receptors reveals previously untargeted allosteric sites

<p>Supplementary Data 1: list of all analysed structures together with the docking files</p> <p>Supplementary Data 2: grid files, template and README for visualising the class-specific density maps by using Pymol</p>

opencc-by-4.0Dec 2021View details →
zenodo32/100

Reproducibility Package for "Design of an allosterically modulated doxycycline and doxorubicin-binding protein"

<p>Files used for MUMBO calculations depicted in the Supplementary Figure 1 of the manuscript &quot;Design of an allosterically modulated doxycycline and doxorubicin-binding protein&quot;</p>

opencc-by-4.0Dec 2017View details →
zenodo28/100

Research and Evaluation of Allosteric Protein Specific Force Field Based on Deep Learning

<p>All trajectories for evaluating&nbsp;APSF force field</p>

opencc-by-4.0Oct 2022View details →
geo24/100

Direct Selection of an Allosteric RNA-Cleaving DNAzyme for a Protein Target: A Specific DNAzyme for Eosinophil Peroxidase to Monitor Airway Eosinopilia

GEO Series GSE217946. synthetic construct. 1 samples. Type: Other.

openGEO-OpenNov 2023View details →
geo24/100

Paraspeckle Protein NONO Regulates Active Chromatin by Allosterically Stimulating NSD1

GEO Series GSE304363. Mus musculus; Homo sapiens. 36 samples. Type: Expression profiling by high throughput sequencing; Genome binding/occupancy profiling by high throughput sequencing.

openGEO-OpenAug 2025View details →
geo24/100

Mrg15 allosterically activates Ash1’s H3K36 methyltransferase activity and facilitates Ash1’s trithorax group protein function in Drosophila

GEO Series GSE93100. Drosophila melanogaster. 21 samples. Type: Genome binding/occupancy profiling by high throughput sequencing; Expression profiling by high throughput sequencing.

openGEO-OpenOct 2017View details →
geo24/100

Global mapping of the energetic and allosteric landscapes of protein binding domains

GEO Series GSE184042. Saccharomyces cerevisiae. 24 samples. Type: Other.

openGEO-OpenSep 2021View details →
geo20/100

Allosteric and Energetic Remodeling by Protein Domain Extensions

GEO Series GSE299757. Saccharomyces cerevisiae. 56 samples. Type: Other.

openGEO-OpenJul 2025View details →

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