Strong cooperativity and loose geometry between CUB domains are the basis for procollagen C-proteinase enhancer activity

Journal of Biological Chemistry

Volumn 284, Issue 48, 2009, Pages 33437-33446

  Kronenberg, Daniel ^a,b   Vadon Le Goff, Sandrine ^a   Bourhis, Jean Marie ^a   Font, Bernard ^a   Eichenberger, Denise ^a   Hulmes, David J S ^a   Moali, Catherine ^a  

^a University Lyon i   (France)

^b JOHANNES GUTENBERG UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOLOGY;

BONE MORPHOGENETIC PROTEINS; COMPLEX FORMATIONS; DISSOCIATION CONSTANT; FIBRILLAR COLLAGENS; NANOMOLAR AFFINITY; PROCOLLAGEN C PROTEINASE; SUBSTRATE BINDING; THREE ORDERS OF MAGNITUDE;

DISSOCIATION;

BINDING PROTEIN; PROCOLLAGEN C PROTEINASE; PROCOLLAGEN C PROTEINASE ENHANCER 1 PROTEIN; PROTEIN CUB1; PROTEIN CUB2; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING SITE; CHIMERA; CONTROLLED STUDY; DELETION MUTANT; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; GEOMETRY; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION;

EID: 70450285123     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.046128     Document Type: Article

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