期刊
PROTEIN ENGINEERING DESIGN & SELECTION
卷 24, 期 4, 页码 405-409出版社
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzq115
关键词
alignment; amyloid; computation; matrix; simulation
资金
- Norwegian Research Council
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.
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