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

Hidong Kim, Stephen K. Burley, William N. Lipscomb

Research output: Contribution to journalEditorial

33 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)722-724
Number of pages3
JournalJournal of molecular biology
Volume230
Issue number3
DOIs
StatePublished - Apr 5 1993
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology

Keywords

  • Bestatin
  • Leucine aminopeptidase
  • X-ray crystallography

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