Solution structure of human Mts1 (S100A4) as determined by NMR spectroscopy

Biochemistry

Volumn 41, Issue 42, 2002, Pages 12670-12680

  Vallely, Kristen M ^a   Rustandi, Richard R ^a   Ellis, Karen C ^a   Varlamova, Olga ^b   Bresnick, Anne R ^b   Weber, David J ^a  

^a UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

TUMOR PROGRESSIONS;

AMINO ACIDS; CONFORMATIONS; DIMERS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; TUMORS;

BIOCHEMISTRY;

CALCIUM BINDING PROTEIN; CALCYCLIN; PROTEIN; PROTEIN MTS; PROTEIN S 100; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONSENSUS SEQUENCE; COVALENT BOND; CRYSTAL STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; APOPROTEINS; CALCIUM-BINDING PROTEINS; DIMERIZATION; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; S100 PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SOLUTIONS; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 0037159217     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi020365r     Document Type: Article

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