title: A geometry-based generic predictor for catalytic and allosteric sites.
abstract: 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.
authors.affiliation: Computational Biology Unit, Bergen Center for Computational Science, Bergen, Norway.
authors.forename: Simon
authors.initials: S
authors.lastname: Mitternacht
authors.forename: Igor N
authors.initials: IN
authors.lastname: Berezovsky
mesh_terms: D000495:Allosteric Site; D020134:Catalytic Domain; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology; D004798:Enzymes / Q000737:chemistry*; D011506:Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry*; D020539:Sequence Analysis, Protein / Q000379:methods*
chemical_list: D004791:Enzyme Inhibitors; D004798:Enzymes; D011506:Proteins