Solution Structure of the Disulfide-Linked Dimer of Human Intestinal Trefoil Factor (TFF3): The Intermolecular Orientation and Interactions Are Markedly Different from Those of Other Dimeric Trefoil Proteins

Biochemistry

Volumn 42, Issue 51, 2003, Pages 15139-15147

  Muskett, Frederick W ^a   May, Felicity E B ^b   Westley, Bruce R ^b   Feeney, James ^a  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

^b NEWCASTLE UNIVERSITY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

MONOMERS; NUCLEAR MAGNETIC RESONANCE; PROTEINS; SOLVENTS;

LIGAND BINDING;

DIMERS;

DIMER; MONOMER; SOLVENT; TREFOIL PEPTIDE;

ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; DIMERIZATION; DISULFIDE BOND; LIGAND BINDING; MOLECULAR INTERACTION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FUNCTION; RECEPTOR BINDING;

AMINO ACID SEQUENCE; ANIMALS; CONSERVED SEQUENCE; CYSTEINE; DIMERIZATION; DISULFIDES; HUMANS; HYDROPHOBICITY; INTESTINES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUCINS; MUSCLE PROTEINS; NEUROPEPTIDES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEINS; SEQUENCE ALIGNMENT; SOLUTIONS; STRUCTURE-ACTIVITY RELATIONSHIP; TUMOR SUPPRESSOR PROTEINS;

LOTUS;

EID: 0348224040     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi030182k     Document Type: Article

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