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2 results for “Chemical Cross-linking”
High-density Chemical Cross-linking for Modeling Protein Interactions
<p>Supporting parameters, IMP code and data for Mintseris & Gygi "High-density Chemical Cross-linking for Modeling Protein Interactions" <em>PNAS</em></p> <p><strong>Parameter Files</strong></p> <p>These parameter files were used for running PIXL to produce the data described in the paper</p> <p><strong>Fasta Sequence Databases</strong></p> <p>These sequence databases were used for running PIXL to produce the data described in the paper</p> <p><strong>IMP</strong></p> <p>Code, intermediate data, and final localization densities for IMP proteasome modeling as described in the paper See IMP directory README</p>
Modeling of the TFIIH complex using chemical cross-links and electron microscopy (EM) density maps
<p>TFIIH is essential for both RNA polymerase II transcription and DNA repair, and mutations in TFIIH can result in human disease. Here, we determine the molecular architecture of human and yeast TFIIH by an integrative approach using chemical crosslinking/mass spectrometry (CXMS) data, biochemical analyses, and previously published electron microscopy maps. We identified four new conserved "topological regions" that function as hubs for TFIIH assembly and more than 35 conserved topological features within TFIIH, illuminating a network of interactions involved in TFIIH assembly and regulation of its activities. We show that one of these conserved regions, the p62/Tfb1 Anchor region, directly interacts with the DNA helicase subunit XPD/Rad3 in native TFIIH and is required for the integrity and function of TFIIH. We also reveal the structural basis for defects in patients with xeroderma pigmentosum and trichothiodystrophy, with mutations found at the interface between the p62 Anchor region and the XPD subunit.</p> <p>For more information about how to reproduce this modeling, see https://salilab.org/tfiih or the README file.</p>
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