Crystallographic studies on the binding modes of P2-P3 butanediamide renin inhibitors.
The binding modes of three peptidomimetic P2-P3 butanediamide renin inhibitors have been determined by x-ray crystallography. The inhibitors are bound with their backbones in an extended conformation, and their side chains occupying the S5 to S1' pockets. A (2-amino-4-thiazolyl)methyl side chain at the P2 position shows stronger hydrogen-bonding and van der Waals interactions with renin than the His side chain, which is present in the natural substrate. The ACHPA-gamma-lactam transition state analog has similar interactions with renin as the dihydroxyethylene transition state analog.
D003461:Crystallography; D003958:Diamide / Q000737:chemistry; D004791:Enzyme Inhibitors / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D000092502:Renin Inhibitors
D003958:Diamide; D004791:Enzyme Inhibitors; D000092502:Renin Inhibitors