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• W1973909424 endingPage "173" @default.
• W1973909424 startingPage "163" @default.
• W1973909424 abstract "Human chymase (HC) is a chymotrypsin-like serine proteinase expressed by mast cells. The 2.2 Å 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 β-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 ϵ-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." @default.
• W1973909424 created "2016-06-24" @default.
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• W1973909424 date "1999-02-01" @default.
• W1973909424 modified "2023-10-16" @default.
• W1973909424 title "The 2.2 å crystal structure of human chymase in complex with succinyl-ala-ala-pro-phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity" @default.
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• W1973909424 doi "https://doi.org/10.1006/jmbi.1998.2462" @default.
• W1973909424 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9931257" @default.
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