NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein

Journal of Molecular Biology

Volumn 301, Issue 4, 2000, Pages 1003-1017

  Sekerina, Elena ^a   Rahfeld, Jens Ulrich ^a   Müller, Jonathan ^a   Fanghänel, Jörg ^a   Rascher, Christine ^a   Fischer, Gunter ^a   Bayer, Peter ^a  

^a MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING   (Germany)

Author keywords

cis trans isomerization; Parvulin; PPIase

Indexed keywords

BACTERIAL PROTEIN; PARVULIN; PEPTIDYL PROLYL ISOMERASE; RECOMBINANT PROTEIN; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CELL CYCLE; CHEMICAL STRUCTURE; ESCHERICHIA COLI; ISOMERISM; NONHUMAN; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SEQUENCE HOMOLOGY; THREE DIMENSIONAL IMAGING;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0034714176     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4013     Document Type: Article

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