The interactions of adenylate cyclases with P-site inhibitors.
Recent kinetic, binding and crystallographic studies using P-site inhibitors of mammalian adenylate bases provide new insights into the catalytic mechanism of these highly regulated enzymes. Here, Carmen Dessauer and colleagues discuss the conformational states of adenylate cyclase, the structural determinants of inhibitor binding and the potential uses of these inhibitors as pharmacological agents.
Dessauer
C W
CW
Department of Integrative Biology, Pharmacology and Physiology, University of Texas Health Science Center at Houston, Houston, TX, USA.
Tesmer
J J
JJ
Sprang
S R
SR
Gilman
A G
AG
D000067956:Adenylyl Cyclase Inhibitors; D000262:Adenylyl Cyclases / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D020134:Catalytic Domain; D003461:Crystallography; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology* / Q000627:therapeutic use; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation
D000067956:Adenylyl Cyclase Inhibitors; D004791:Enzyme Inhibitors; D000262:Adenylyl Cyclases