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[[Image:1pjp.gif|left|200px]]
{{Seed}}
[[Image:1pjp.png|left|200px]]


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{{STRUCTURE_1pjp|  PDB=1pjp  |  SCENE=  }}  
{{STRUCTURE_1pjp|  PDB=1pjp  |  SCENE=  }}  


'''THE 2.2 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN COMPLEX WITH SUCCINYL-ALA-ALA-PRO-PHE-CHLOROMETHYLKETONE'''
===THE 2.2 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN COMPLEX WITH SUCCINYL-ALA-ALA-PRO-PHE-CHLOROMETHYLKETONE===




==Overview==
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Human chymase (HC) is a chymotrypsin-like serine proteinase expressed by mast cells. The 2.2 A crystal structure of HC complexed to the peptidyl inhibitor, succinyl-Ala-Ala-Pro-Phe-chloromethylketone (CMK), was solved and refined to a crystallographic R-factor of 18.4 %. The HC structure exhibits the typical folding pattern of a chymotrypsin-like serine proteinase, and shows particularly similarity to rat chymase 2 (rat mast cell proteinase II) and human cathepsin G. The peptidyl-CMK inhibitor is covalently bound to the active-site residues Ser195 and His57; the peptidyl moiety juxtaposes the S1 entrance frame segment 214-217 by forming a short antiparallel beta-sheet. HC is a highly efficient angiotensin-converting enzyme. Modeling of the chymase-angiotensin I interaction guided by the geometry of the bound chloromethylketone inhibitor indicates that the extended substrate binding site contains features that may generate the dipeptidyl carboxypeptidase-like activity needed for efficient cleavage and activation of the hormone. The C-terminal carboxylate group of angiotensin I docked into the active-site cleft, with the last two residues extending beyond the active site, is perfectly localized to make a favorable hydrogen bond and salt bridge with the amide nitrogen of the Lys40-Phe41 peptide bond and with the epsilon-ammonium group of the Lys40 side-chain. This amide positioning is unique to the chymase-related proteinases, and only chymases from primates possess a Lys residue at position 40. Thus, the structure conveniently explains the preferred conversion of angiotensin I to angiotensin II by human chymase.
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{{ABSTRACT_PUBMED_9931257}}


==About this Structure==
==About this Structure==
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[[Category: Human chymase]]
[[Category: Human chymase]]
[[Category: Serine proteinase]]
[[Category: Serine proteinase]]
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Revision as of 15:06, 27 July 2008

File:1pjp.png

Template:STRUCTURE 1pjp

THE 2.2 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN COMPLEX WITH SUCCINYL-ALA-ALA-PRO-PHE-CHLOROMETHYLKETONE

Template:ABSTRACT PUBMED 9931257

About this Structure

1PJP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The 2.2 A crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity., Pereira PJ, Wang ZM, Rubin H, Huber R, Bode W, Schechter NM, Strobl S, J Mol Biol. 1999 Feb 12;286(1):163-73. PMID:9931257

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