Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond

Science. 1987 Jan 30;235(4788):571-4. doi: 10.1126/science.3810156.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amides
  • Crystallography
  • Esters
  • Hydrogen Bonding
  • Molecular Conformation
  • Oligopeptides / pharmacology
  • Organophosphonates
  • Thermodynamics
  • Thermolysin / antagonists & inhibitors*
  • X-Ray Diffraction


  • Amides
  • Esters
  • Oligopeptides
  • Organophosphonates
  • Thermolysin