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The structural basis of allosteric regulation in proteins

Laskowski, R.A. and Gerick, F. and Thornton, Janet M. (2009) The structural basis of allosteric regulation in proteins. FEBS Letters 583 (11), pp. 1692-1698. ISSN 1873-3468.

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Official URL: http://dx.doi.org/10.1016/j.febslet.2009.03.019

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 Å, or tens of Å. 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.

Item Type: Article
School or Research Centre: Birkbeck Schools and Research Centres > School of Science > Biological Sciences
Depositing User: Administrator
Date Deposited: 04 Aug 2010 14:09
Last Modified: 17 Apr 2013 12:17
URI: http://eprints.bbk.ac.uk/id/eprint/1127

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