Allosteric regulation of proteases.
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.
Hauske
Patrick
P
Chemical Genomics Centre der Max-Planck-Gesellschaft, Dortmund, Germany.
Ottmann
Christian
C
Meltzer
Michael
M
Ehrmann
Michael
M
Kaiser
Markus
M
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
D061945:Caspase Inhibitors; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; D020169:Caspases