1hdq: Difference between revisions

Revision as of 08:02, 1 July 2008

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File:1hdq.png

Template:STRUCTURE 1hdq

CRYSTAL STRUCTURE OF BOVINE PANCREATIC CARBOXYPEPTIDASE A COMPLEXED WITH D-N-HYDROXYAMINOCARBONYL PHENYLALANINE AT 2.3 ACRYSTAL STRUCTURE OF BOVINE PANCREATIC CARBOXYPEPTIDASE A COMPLEXED WITH D-N-HYDROXYAMINOCARBONYL PHENYLALANINE AT 2.3 A

Template:ABSTRACT PUBMED 11937361

About this StructureAbout this Structure

1HDQ is a Single protein structure of sequence from Bos taurus. 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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OCA

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-'''CRYSTAL STRUCTURE OF BOVINE PANCREATIC CARBOXYPEPTIDASE A COMPLEXED WITH D-N-HYDROXYAMINOCARBONYL PHENYLALANINE AT 2.3 A'''
+===CRYSTAL STRUCTURE OF BOVINE PANCREATIC CARBOXYPEPTIDASE A COMPLEXED WITH D-N-HYDROXYAMINOCARBONYL PHENYLALANINE AT 2.3 A===
-==Overview==
+<!--
-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 involved in interactions with the active site zinc ion and the carboxylate of Glu-270. In both CPA small middle dot complexes, the phenyl ring in is fitted in the substrate recognition pocket at the S(1)' subsite, and the carboxylate of the inhibitors forms bifurcated hydrogen bonds with the guanidinium moiety of Arg-145 and a hydrogen bond with the guanidinium of Arg-127. In the complex of CPA small middle dotD-, the carboxylate of the inhibitor is engaged in hydrogen bonding with the phenolic hydroxyl of the down-positioned Tyr-248. While the L- binding induces a concerted movement of the backbone amino acid residues at the active site, only the downward movement of Tyr-248 was noted when D- binds to CPA.
+The line below this paragraph, {{ABSTRACT_PUBMED_11937361}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Inhibitor]]
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