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Allosteric regulation of proteases

Hauske, Patrick, Ottmann, Christian, Meltzer, Michael, Ehrmann, Michael and Kaiser, Markus 2008. Allosteric regulation of proteases. Chembiochem 9 (18) , pp. 2920-2928. 10.1002/cbic.200800528

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Abstract

Allostery is a basic principle of control of enzymatic activities based on the interaction of a protein or small molecule at a site distinct from an enzyme's active center. Allosteric modulators represent an alternative approach to the design and synthesis of small-molecule activators or inhibitors of proteases and are therefore of wide interest for medicinal chemistry. The structural bases of some proteinaceous and small-molecule allosteric protease regulators have already been elucidated, indicating a general mechanism that might be exploitable for future rational design of small-molecule effectors

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Subjects: Q Science > QD Chemistry
Q Science > QP Physiology
Publisher: Wiley-Blackwell
ISSN: 1439-4227
Last Modified: 04 Jun 2017 06:15
URI: http://orca.cf.ac.uk/id/eprint/57791

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