牛晶状体亮氨酸氨肽酶与贝他定复合物的X射线晶体结构的重新精修
Re-refinement of the X-ray crystal structure of bovine lens leucine aminopeptidase complexed with bestatin.
作者信息
Kim H, Burley S K, Lipscomb W N
机构信息
Gibbs Chemical Laboratory, Harvard University, Cambridge, MA 02138.
出版信息
J Mol Biol. 1993 Apr 5;230(3):722-4. doi: 10.1006/jmbi.1993.1193.
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.
贝抑素，即(2S,3R)-3-氨基-2-羟基-4-苯基丁酰-L-亮氨酸，在先前报道的牛晶状体亮氨酸氨肽酶（blLAP）与贝抑素复合物结构中建模错误。在先前报道的结构中，贝抑素的C2被建模并精修为R构型，而非正确的S构型。在将贝抑素重塑为正确的立体化学结构后，对blLAP-贝抑素复合物的结构进行了重新精修。
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