Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer

Structure

Volumn 9, Issue 6, 2001, Pages 457-471

  Liepinsh, E ^a   Baryshev, M ^a,b   Sharipo, A ^b   Ingelman Sundberg, M ^a   Otting, G ^a   Mkrtchian, S ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

^b LATVIAN BIOMEDICAL RESEARCH AND STUDY CENTRE   (Latvia)

Author keywords

Chaperone; ERp29; Homodimer; NMR spectroscopy; Protein disulfide isomerase; Thioredoxin

Indexed keywords

CELL PROTEIN; DIMER; OLIGOMER; PROTEIN DISULFIDE ISOMERASE; PROTEIN ERP29; THIOREDOXIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; COVALENT BOND; DIMERIZATION; EXPERIMENTAL MODEL; MOLECULAR INTERACTION; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FOLDING; THREE DIMENSIONAL IMAGING;

AMINO ACID SEQUENCE; DIMERIZATION; ENDOPLASMIC RETICULUM; HEAT-SHOCK PROTEINS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE HOMOLOGY, AMINO ACID; THIOREDOXIN;

EUKARYOTA; MAMMALIA;

EID: 0034989106     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(01)00607-4     Document Type: Article

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