GWYRE: A resource for mapping variants onto experimental and modeled structures of human protein complexes
File(s)
Supporting information
Published version
Author(s)
Type
Journal Article
Abstract
Rapid progress in structural modeling of proteins and their interactions is powered by advances in knowledge-based methodologies along with better understanding of physical principles of protein structure and function. The pool of structural data for modeling of proteins and protein–protein complexes is constantly increasing due to the rapid growth of protein interaction databases and Protein Data Bank. The GWYRE (Genome Wide PhYRE) project capitalizes on these developments by advancing and applying new powerful modeling methodologies to structural modeling of protein–protein interactions and genetic variation. The methods integrate knowledge-based tertiary structure prediction using Phyre2 and quaternary structure prediction using template-based docking by a full-structure alignment protocol to generate models for binary complexes. The predictions are incorporated in a comprehensive public resource for structural characterization of the human interactome and the location of human genetic variants. The GWYRE resource facilitates better understanding of principles of protein interaction and structure/function relationships. The resource is available at http://www.gwyre.org.
Date Issued
2022-06-15
Date Acceptance
2022-04-20
Citation
Journal of Molecular Biology, 2022, 434 (11)
ISSN
0022-2836
Publisher
Elsevier
Journal / Book Title
Journal of Molecular Biology
Volume
434
Issue
11
Copyright Statement
© 2022 The Authors. Published by Elsevier Ltd.This is an open access article under the CC BY license (http://creativecommons.org/licenses/
by/4.0/).
by/4.0/).
License URL
Sponsor
Wellcome Trust
Biotechnology and Biological Sciences Research Council (BBSRC)
Wellcome Trust
Identifier
https://www.sciencedirect.com/science/article/pii/S0022283622001887
Grant Number
WT/104955/Z/14/Z
BB/T010487/1
218242/Z/19/Z
Subjects
amino acid mutations
genome-wide modeling
genotype to phenotype
protein docking
structure prediction
Binding Sites
Computational Biology
Databases, Protein
Humans
Molecular Docking Simulation
Protein Binding
Protein Interaction Mapping
Proteins
Software
Humans
Proteins
Protein Interaction Mapping
Computational Biology
Binding Sites
Protein Binding
Software
Databases, Protein
Molecular Docking Simulation
0304 Medicinal and Biomolecular Chemistry
0601 Biochemistry and Cell Biology
0605 Microbiology
Biochemistry & Molecular Biology
Publication Status
Published
Article Number
ARTN 167608
Date Publish Online
2022-04-27