Insights into how CUB domains can exert specific functions while sharing a common fold: Conserved and specific features of the CUB1 domain contribute to the molecular basis of procollagen C-proteinase enhancer-1 activity

Journal of Biological Chemistry

Volumn 282, Issue 23, 2007, Pages 16924-16933

  Blanc, Guillaume ^a   Font, Bernard ^a   Eichenberger, Denise ^a   Moreau, Christophe ^a,b   Ricard Blum, Sylvie ^a   Hulmes, David J S ^a   Moali, Catherine ^a  

^a University Lyon i   (France)

^b CEA GRENOBLE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL MEMBRANES; COLLAGEN; ENZYME ACTIVITY; SURFACE PLASMON RESONANCE;

ANTI-FIBROTIC THERAPIES; CALCIUM BINDING MOTIF; FIBRILLAR PROCOLLAGENS; PROCOLLAGEN C-PROTEINASE ENHANCERS;

PROTEIN FOLDING;

ALANINE; AMINO ACID; ANTIFIBROTIC AGENT; CALCIUM; PROCOLLAGEN C PROTEINASE; TYROSINE; BONE MORPHOGENETIC PROTEIN; METALLOPROTEINASE; PRIMER DNA;

ARTICLE; BINDING SITE; ENZYME ACTIVITY; MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; SURFACE PLASMON RESONANCE; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; ENHANCER REGION; FLUORESCENCE; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN BINDING; PROTEIN FOLDING; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; BASE SEQUENCE; BONE MORPHOGENETIC PROTEINS; CIRCULAR DICHROISM; CONSERVED SEQUENCE; DNA PRIMERS; ENHANCER ELEMENTS (GENETICS); FLUORESCENCE; HUMANS; METALLOENDOPEPTIDASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN FOLDING; SEQUENCE HOMOLOGY, AMINO ACID; SURFACE PLASMON RESONANCE;

EID: 34447125072     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M701610200     Document Type: Article

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