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

Journal of Molecular Biology

Volumn 286, Issue 1, 1999, Pages 163-173

  Pereira, Pedro José Barbosa ^a   Wang, Zhi Mei ^b   Rubin, Harvey ^b   Huber, Robert ^a   Bode, Wolfram ^a   Schechter, Norman M ^b   Strobl, Stefan ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Angiotensin; Dipeptidyl carboxypeptidase; Human chymase; Serine proteinase; X ray crystallography

Indexed keywords

ANGIOTENSIN; CHYMASE; DIPEPTIDYL CARBOXYPEPTIDASE; SERINE PROTEINASE; ENZYME INHIBITOR; OLIGOPEPTIDE; PEPTIDE CHLOROMETHYL KETONE; PROTEINASE; PROTEINASE INHIBITOR; RECOMBINANT PROTEIN; SUCCINYL ALANYLALANYL PROLYL PHENYLALANINE CHLOROMETHYLKETONE; SUCCINYL-ALANYLALANYL-PROLYL-PHENYLALANINE CHLOROMETHYLKETONE;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; HYDROGEN BOND; MAST CELL; PRIORITY JOURNAL; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID CHLOROMETHYL KETONES; AMINO ACID SEQUENCE; CHYMASES; CRYSTALLOGRAPHY, X-RAY; ENDOPEPTIDASES; ENZYME INHIBITORS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; PROTEASE INHIBITORS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY;

EID: 0033547878     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2462     Document Type: Article

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