title: Allosteric regulation of proteases.
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.
authors.affiliation: Chemical Genomics Centre der Max-Planck-Gesellschaft, Dortmund, Germany.
authors.forename: Patrick
authors.initials: P
authors.lastname: Hauske
authors.forename: Christian
authors.initials: C
authors.lastname: Ottmann
authors.forename: Michael
authors.initials: M
authors.lastname: Meltzer
authors.forename: Michael
authors.initials: M
authors.lastname: Ehrmann
authors.forename: Markus
authors.initials: M
authors.lastname: Kaiser
mesh_terms: D000494:Allosteric Regulation; D061945:Caspase Inhibitors; D020169:Caspases / Q000737:chemistry / Q000378:metabolism; D002626:Chemistry, Pharmaceutical; D018360:Crystallography, X-Ray; D015195:Drug Design; D008958:Models, Molecular; D010447:Peptide Hydrolases / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D061945:Caspase Inhibitors; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; D020169:Caspases