Kim_1993_J.Mol.Biol_230_722

Reference

Title : Re-refinement of the X-ray crystal structure of bovine lens leucine aminopeptidase complexed with bestatin - Kim_1993_J.Mol.Biol_230_722
Author(s) : Kim H , Burley SK , Lipscomb WN
Ref : Journal of Molecular Biology , 230 :722 , 1993
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.

PubMedSearch : Kim_1993_J.Mol.Biol_230_722
PubMedID: 8478928

Related information

Citations formats

Kim H, Burley SK, Lipscomb WN (1993)
Re-refinement of the X-ray crystal structure of bovine lens leucine aminopeptidase complexed with bestatin
Journal of Molecular Biology 230 :722

Kim H, Burley SK, Lipscomb WN (1993)
Journal of Molecular Biology 230 :722