title: Re-refinement of the X-ray crystal structure of bovine lens leucine aminopeptidase complexed with bestatin.
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.
authors: Gibbs Chemical Laboratory, Harvard University, Cambridge, MA 02138.
authors: H
authors: H
authors: Kim
authors: S K
authors: SK
authors: Burley
authors: W N
authors: WN
authors: Lipscomb
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D007908:Lens, Crystalline / Q000201:enzymology*; D007930:Leucine / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D007931:Leucyl Aminopeptidase / Q000737:chemistry* / Q000378:metabolism; D015394:Molecular Structure; D014961:X-Ray Diffraction
chemical_list: D007931:Leucyl Aminopeptidase; D007930:Leucine; C012211:ubenimex