A geometry-based generic predictor for catalytic and allosteric sites
TypeJournal article; Peer reviewed
MetadataShow full item record
An important aspect of understanding protein allostery, and of artificial effector design, is the characterization and prediction of substrate- and effector-binding sites. To find binding sites in allosteric enzymes, many of which are oligomeric with allosteric sites at domain interfaces, we devise a local centrality measure for residue interaction graphs, which behaves well for both small/monomeric and large/multimeric proteins. The measure is purely structure based and has a clear geometrical interpretation and no free parameters. It is not biased towards typically catalytic residues, a property that is crucial when looking for non-catalytic effector sites, which are potent drug targets.
CitationProtein Engineering, Design and Selection 24(4): 405-409
PublisherOxford University Press
SubjectAllosteryallosteric regulationcatalytic sitesbinding sitessite predictionlocal closenessProtein structureEnzyme
Copyright the Author 2010. Published by Oxford University Press. All rights reserved.