Characterization of high affinity binding motifs for the discoidin domain receptor DDR2 in collagen

Journal of Biological Chemistry

Volumn 283, Issue 11, 2008, Pages 6861-6868

  Konitsiotis, Antonios D ^a   Raynal, Nicolas ^c   Bihan, Dominique ^c   Hohenester, Erhard ^b   Farndale, Richard W ^c   Leitinger, Birgit ^a,b  

^a NATIONAL HEART AND LUNG INSTITUTE   (United Kingdom)

^b IMPERIAL COLLEGE LONDON   (United Kingdom)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING MOTIFS; COLLAGEN BINDINGS; COLLAGEN II; COLLAGEN SEQUENCES; DO-MAINS; FIBRILLAR COLLAGENS; HELICAL CONFORMATIONS; HELICAL DOMAINS; HELICAL PEPTIDES; HIGH AFFINITY BINDINGS; NMR ANALYSES; PEPTIDE SEQUENCES; RECEPTOR TYROSINE KINASES; TRANSMEMBRANE SIGNALING; VON WILLEBRAND FACTORS;

AMINES; AMINO ACIDS; BINDING ENERGY; BIOCHEMISTRY; COLLAGEN; NUCLEAR MAGNETIC RESONANCE; PEPTIDES; PROTEINS;

BINDING SITES;

ALANINE; COLLAGEN; COLLAGEN TYPE 2; COLLAGEN TYPE 3; DISCOIDIN DOMAIN RECEPTOR 2; FIBRILLAR COLLAGEN; HYDROXYPROLINE; RECEPTOR PROTEIN; UNCLASSIFIED DRUG; VON WILLEBRAND FACTOR; DISCOIDIN RECEPTOR; LECTIN RECEPTOR; PEPTIDE; PROTEIN TYROSINE KINASE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANALYZER; ARTICLE; BINDING AFFINITY; BINDING SITE; EMBRYO; HUMAN; HUMAN CELL; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN LOCALIZATION; PROTEIN MOTIF; RECEPTOR BINDING; RECEPTOR UPREGULATION; SIGNAL TRANSDUCTION; TRIPLE HELIX; ANIMAL; CATTLE; CELL MEMBRANE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE; RAT;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CATTLE; CELL MEMBRANE; COLLAGEN; HUMANS; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RATS; RECEPTOR PROTEIN-TYROSINE KINASES; RECEPTORS, MITOGEN; VON WILLEBRAND FACTOR;

EID: 42449119742     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M709290200     Document Type: Article

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