allosteric site


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Related to allosteric site: competitive inhibition

allosteric

 [al″o-ster´ik]
pertaining to an effect produced on the biological function of a protein by a compound not directly involved in that function (an allosteric effector) or to regulation of an enzyme involving cooperativity between multiple binding sites (allosteric sites).
allosteric site that subunit of an enzyme molecule which binds with a nonsubstrate molecule, inducing a change in form or shape that results in inactivation of the enzyme for its substrate.
Miller-Keane Encyclopedia and Dictionary of Medicine, Nursing, and Allied Health, Seventh Edition. © 2003 by Saunders, an imprint of Elsevier, Inc. All rights reserved.

al·lo·ste·ric site

postulated as the place on an enzyme, other than the active site, where a compound, which may be the ultimate product of the biosynthetic pathway involving the enzyme, may bind and influence the activity of the enzyme by changing the enzyme's conformation; the influence of CTP on aspartate carbamoyltransferase activity exemplifies the concept of an allosteric site on an allosteric protein.
Farlex Partner Medical Dictionary © Farlex 2012

al·lo·ste·ric site

(al'ō-ster'ik sīt)
Postulated as the place on an enzyme, other than the active site, where a compound, which may be the ultimate product of the biosynthetic pathway involving the enzyme, may bind and influence the activity of the enzyme by changing the enzyme's conformation.
Medical Dictionary for the Health Professions and Nursing © Farlex 2012

allosteric site

a functional on/off switch for an enzyme situated away from its active site.
Collins Dictionary of Biology, 3rd ed. © W. G. Hale, V. A. Saunders, J. P. Margham 2005
References in periodicals archive ?
A grid with dimensions 100x100x100 with center x = -0.254, y = 11.832 and z = -24.015 was used for targeted docking in the allosteric site of NS2B-NS3.
For example, residue centrality as a local network parameter was proposed to identify allosteric sites [76], and coefficient of assortativity as a global network parameter is related to the rates of protein folding [77].
Hocker et al., "Novel allosteric sites on ras for lead generation," PLoS ONE, vol.
The structures of allosteric sites have been reported for [M.sub.2] and [M.sub.3] receptors, and are expected to be reported for [M.sub.1],[M.sub.4] and [M.sub.5] receptors in the near future.