Re-refinement of the X-ray crystal structure of bovine lens leucine aminopeptidase complexed with bestatin

J Mol Biol. 1993 Apr 5;230(3):722-4. doi: 10.1006/jmbi.1993.1193.

Abstract

Bestatin, (2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-leucine, has been incorrectly modelled in the previously reported structure of the complex between bovine lens leucine aminopeptidase (blLAP) and bestatin. In the previously reported structure, the C2 of bestatin was modelled and refined in the R configuration instead of the correct S configuration. The structure of the blLAP-bestatin complex has been re-refined after remodelling bestatin in its correct stereochemistry.

Publication types

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

MeSH terms

  • Animals
  • Binding Sites
  • Cattle
  • Lens, Crystalline / enzymology*
  • Leucine / analogs & derivatives*
  • Leucine / chemistry
  • Leucine / metabolism
  • Leucyl Aminopeptidase / chemistry*
  • Leucyl Aminopeptidase / metabolism
  • Molecular Structure
  • X-Ray Diffraction

Substances

  • Leucyl Aminopeptidase
  • Leucine
  • ubenimex