Allosteric regulation of protease activity by small molecules.
Proteases regulate a plethora of biological processes. Because they irreversibly cleave peptide bonds, the activity of proteases is strictly controlled. While there are many ways to regulate protease activity, an emergent mechanism is the modulation of protease function by small molecules acting at allosteric sites. This mode of regulation holds the potential to allow for the specific and temporal control of a given biological process using small molecules. These compounds also serve as useful tools for studying protein dynamics and function. This review highlights recent advances in identifying and characterizing natural and synthetic small molecule allosteric regulators of proteases and discusses their utility in studies of protease function, drug discovery and protein engineering.
Shen
Aimee
A
Department of Pathology, Stanford School of Medicine, Stanford, California 94305, USA. ashen2@stanford.edu
D000494:Allosteric Regulation / Q000187:drug effects*; D000495:Allosteric Site / Q000187:drug effects; D000818:Animals; D001427:Bacterial Toxins / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D006801:Humans; D008024:Ligands; D008954:Models, Biological; D008958:Models, Molecular; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000378:metabolism*; D054852:Small Molecule Libraries / Q000494:pharmacology
D001427:Bacterial Toxins; D008024:Ligands; D054852:Small Molecule Libraries; D010447:Peptide Hydrolases