{Reference Type}: Journal Article
{Title}: GWYRE: A Resource for Mapping Variants onto Experimental and Modeled Structures of Human Protein Complexes.
{Author}: Malladi S;Powell HR;David A;Islam SA;Copeland MM;Kundrotas PJ;Sternberg MJE;Vakser IA;
{Journal}: J Mol Biol
{Volume}: 434
{Issue}: 11
{Year}: 06 2022 15
{Factor}: 6.151
{DOI}: 10.1016/j.jmb.2022.167608
{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.