The x-ray crystal structure of human aminopeptidase N reveals a novel dimer and the basis for peptide processing

Journal of Biological Chemistry

Volumn 287, Issue 44, 2012, Pages 36804-36813

  Wong, Alan H M ^a   Zhou, Dongxia ^a   Rini, James M ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO PEPTIDASE; CELL SURFACES; CONFORMATIONAL CHANGE; DIMER STRUCTURE; INHIBITOR COMPLEX; PEPTIDE PROCESSING; X RAY CRYSTAL STRUCTURES;

CELL ADHESION; CELL MEMBRANES; MOLECULAR BIOLOGY; SIGNAL TRANSDUCTION;

PEPTIDES;

AMASTATIN; ANGIOTENSIN II [3-8]; BESTATIN; MICROSOMAL AMINOPEPTIDASE;

ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME INHIBITOR INTERACTION; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN PROCESSING; SIGNAL TRANSDUCTION; X RAY ANALYSIS;

AMINO ACID MOTIFS; ANGIOTENSINS; ANTIGENS, CD13; CATALYTIC DOMAIN; COORDINATION COMPLEXES; CRYSTALLOGRAPHY, X-RAY; HEK293 CELLS; HUMANS; KINETICS; LEUCINE; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PEPTIDES; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, QUATERNARY; PROTEOLYSIS; SIGNAL TRANSDUCTION; SUBSTRATE SPECIFICITY; ZINC;

EID: 84868148624     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.398842     Document Type: Article

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