Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond.
The mode of binding to thermolysin of the ester analog Cbz-GlyP-(O)-Leu-Leu has been determined by x-ray crystallography and shown to be virtually identical (maximum difference 0.2 angstrom) with the corresponding peptide analog Cbz-GlyP-(NH)-Leu-Leu. The two inhibitors provide a matched pair of enzyme-inhibitor complexes that differ by 4.1 kilocalories per mole in intrinsic binding energy but are essentially identical except for the presence or absence of a specific hydrogen bond.
D000577:Amides; D003461:Crystallography; D004952:Esters; D006860:Hydrogen Bonding; D008968:Molecular Conformation; D009842:Oligopeptides / Q000494:pharmacology; D063065:Organophosphonates; D013816:Thermodynamics; D013820:Thermolysin / Q000037:antagonists & inhibitors*; D014961:X-Ray Diffraction
D000577:Amides; D004952:Esters; D009842:Oligopeptides; D063065:Organophosphonates; D013820:Thermolysin