Extensive contacts between ADAMTS13 exosites and von Willebrand factor domain A2 contribute to substrate specificity

Blood

Volumn 112, Issue 5, 2008, Pages 1713-1719

  Gao, Weiqiang ^a   Anderson, Patricia J ^a   Sadler, J Evan ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CYSTEINE; GLUTAMINE; METALLOPROTEINASE; THROMBOSPONDIN 1; VON WILLEBRAND FACTOR; VON WILLEBRAND FACTOR CLEAVING PROTEINASE; ADAM PROTEIN; ADAMTS13 PROTEIN, HUMAN; HYBRID PROTEIN; PEPTIDE FRAGMENT; PRIMER DNA; TRANSCRIPTION FACTOR; TUMOR MARKER; VWA2 PROTEIN, HUMAN;

ARTICLE; ENZYME SPECIFICITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; AMINO ACID SEQUENCE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; GENE DELETION; GENETICS; HUMAN; IN VITRO STUDY; KINETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

ADAM PROTEINS; AMINO ACID SEQUENCE; BASE SEQUENCE; BINDING SITES; DNA PRIMERS; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE DELETION; SUBSTRATE SPECIFICITY; TRANSCRIPTION FACTORS; TUMOR MARKERS, BIOLOGICAL;

EID: 52649182049     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2008-04-148759     Document Type: Article

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