1hdq: Difference between revisions
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CRYSTAL STRUCTURE OF BOVINE PANCREATIC CARBOXYPEPTIDASE A COMPLEXED WITH D-N-HYDROXYAMINOCARBONYL PHENYLALANINE AT 2.3 A
OverviewOverview
Both D- and L-isomers of N-(hydroxyaminocarbonyl)phenylalanine () were, shown to have strong binding affinity towards carboxypeptidase A (CPA), with D- being more potent than its enantiomer by 3-fold (Chung, S. J.;, Kim, D. H. Bioorg. Med. Chem. 2001, 9, 185.). In order to understand the, reversed stereochemical preference shown in the CPA inhibition, we have, solved the crystal structures of CPA complexed with each enantiometer of, up to 1.75 A resolution. Inhibitor L- whose stereochemistry belongs to the, stereochemical series of substrate binds CPA like substrate does with its, carbonyl oxygen coordinating to the active site zinc ion. Its hydroxyl is, engaged in hydrogen bonding with the carboxylate of Glu-270. On the other, hand, in binding of D- to CPA, its terminal hydroxyl group is ... [(full description)]
About this StructureAbout this Structure
1HDQ is a [Single protein] structure of sequence from [Bos taurus] with ZN and INF as [ligands]. Active as [Carboxypeptidase A], with EC number [3.4.17.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Insight into the stereochemistry in the inhibition of carboxypeptidase A with N-(hydroxyaminocarbonyl)phenylalanine: binding modes of an enantiomeric pair of the inhibitor to carboxypeptidase A., Cho JH, Kim DH, Chung SJ, Ha NC, Oh BH, Yong Choi K, Bioorg Med Chem. 2002 Jun;10(6):2015-22. PMID:11937361
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