title: Diversity of allosteric regulation in proteases.
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.
authors.affiliation: Department of Microbiology II, Center for Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, Universtitätsstr 2, 45117 Essen, Germany.
authors.forename: Melisa
authors.initials: M
authors.lastname: Merdanovic
authors.forename: Timon
authors.initials: T
authors.lastname: Mönig
authors.forename: Michael
authors.initials: M
authors.lastname: Ehrmann
authors.forename: Markus
authors.initials: M
authors.lastname: Kaiser
mesh_terms: D000494:Allosteric Regulation / Q000187:drug effects; D055808:Drug Discovery; D006801:Humans; D010447:Peptide Hydrolases / Q000737:chemistry / Q000145:classification / Q000494:pharmacology
chemical_list: D010447:Peptide Hydrolases