The peptide-substrate-binding domain of human collagen prolyl 4-hydroxylases: Backbone assignments, secondary structure, and binding of proline-rich peptides

Journal of Biological Chemistry

Volumn 278, Issue 37, 2003, Pages 34966-34974

  Hieta, Reija ^a   Kukkola, Liisa ^a   Permi, Perttu ^b   Pirilä, Päivi ^a   Kivirikko, Kari I ^a   Kilpeläinen, Ilkka ^b   Myllyharju, Johanna ^a  

^a UNIVERSITY OF OULU   (Finland)

^b UNIVERSITY OF HELSINKI   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

CALORIMETRY; CATALYSIS; ENZYMES; POLYPEPTIDES; SURFACE PLASMON RESONANCE; TITRATION;

CHEMICAL SHIFTS;

BIOCHEMISTRY;

COLLAGEN; ENZYME; HYDROXYPROLINE; PEPTIDE; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROLINE; TETRAMER; TYROSINE;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; ENZYME BINDING; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBUNIT; HUMAN; HYDROPHOBICITY; HYDROXYLATION; ISOMER; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; BINDING SITES; CIRCULAR DICHROISM; COLLAGEN; HUMANS; MOLECULAR SEQUENCE DATA; PEPTIDES; PROCOLLAGEN-PROLINE DIOXYGENASE; PROLINE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

VERTEBRATA;

EID: 0042818299     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M303624200     Document Type: Article

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