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A geometry-based generic predictor for catalytic and allosteric sites

Mitternacht, Simon; Berezovsky, Igor N.
Peer reviewed, Journal article
Accepted version
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URI
https://hdl.handle.net/1956/6173
Date
2011
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  • Department of Informatics [536]
Original version
Protein Engineering, Design and Selection 24(4): 405-409   https://doi.org/10.1093/protein/gzq115
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.
Publisher
Oxford University Press
Copyright
Copyright the Author 2010. Published by Oxford University Press. All rights reserved.

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