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FEBS Lett. 2009 Jun 5;583(11):1692-8. doi: 10.1016/j.febslet.2009.03.019. Epub 2009 Mar 18.

The structural basis of allosteric regulation in proteins.

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  • 1European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, United Kingdom. roman@ebi.ac.uk

Abstract

Allosteric regulation of protein function occurs when the regulatory trigger, such as the binding of a small-molecule effector or inhibitor, takes place some distance from the protein's, or protein complex's, active site. This distance can be a few A, or tens of A. Many proteins are regulated in this way and exhibit a variety of allosteric mechanisms. Here we review how analyses of experimentally determined models of protein 3D structures, using either X-ray crystallography or NMR spectroscopy, have revealed some of the mechanisms involved.

PMID:
19303011
[PubMed - indexed for MEDLINE]
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