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Diversity of allosteric regulation in proteases

ACS Chem Biol. 2013 Jan 18;8(1):19-26. doi: 10.1021/cb3005935. Epub 2012 Dec 3.

Abstract

Allostery is a fundamental regulatory mechanism that is based on a functional modulation of a site by a distant site. Allosteric regulation can be triggered by binding of diverse allosteric effectors, ranging from small molecules to macromolecules, and is therefore offering promising opportunities for functional modulation in a wide range of applications including the development of chemical probes or drug discovery. Here, we provide an overview of key classes of allosteric protease effectors, their corresponding molecular mechanisms, and their practical implications.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Allosteric Regulation / drug effects
  • Drug Discovery
  • Humans
  • Peptide Hydrolases* / chemistry
  • Peptide Hydrolases* / classification
  • Peptide Hydrolases* / pharmacology

Substances

  • Peptide Hydrolases