1hdu
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1hdu.jpg|left|200px]] | [[Image:1hdu.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1hdu", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1hdu| PDB=1hdu | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''CRYSTAL STRUCTURE OF BOVINE PANCREATIC CARBOXYPEPTIDASE A COMPLEXED WITH AMINOCARBONYLPHENYLALANINE AT 1.75 A''' | '''CRYSTAL STRUCTURE OF BOVINE PANCREATIC CARBOXYPEPTIDASE A COMPLEXED WITH AMINOCARBONYLPHENYLALANINE AT 1.75 A''' | ||
| Line 32: | Line 29: | ||
[[Category: Kim, D H.]] | [[Category: Kim, D H.]] | ||
[[Category: Oh, B H.]] | [[Category: Oh, B H.]] | ||
| - | [[Category: | + | [[Category: Cpa]] |
| - | [[Category: | + | [[Category: Inhibitor]] |
| - | [[Category: | + | [[Category: Lbhb]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:44:46 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:44, 2 May 2008
CRYSTAL STRUCTURE OF BOVINE PANCREATIC CARBOXYPEPTIDASE A COMPLEXED WITH AMINOCARBONYLPHENYLALANINE AT 1.75 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.
About this Structure
1HDU is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 18:44:46 2008
Categories: Bos taurus | Carboxypeptidase A | Single protein | Cho, J H. | Choi, K Y. | Chung, S J. | Ha, N C. | Kim, D H. | Oh, B H. | Cpa | Inhibitor | Lbhb
