PinA from Aspergillus nidulans binds to pS/pT-P motifs using the same Loop I and XP groove as mammalian Pin1

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1774, Issue 9, 2007, Pages 1208-1212

  Kato, Yusuke ^a,b   Ng, Chai Ann ^c   Brownlee, Robert T C ^c   Tanokura, Masaru ^b  

^a NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c LA TROBE UNIVERSITY   (Australia)

Author keywords

NMR; p patch; PinA; WW domain; XP groove

Indexed keywords

ARGININE; ASPARAGINE; ISOMERASE; LIGAND; PEPTIDYLPROLYL ISOMERASE PIN1; PROLINE; PROTEIN PINA; SERINE; THREONINE; UNCLASSIFIED DRUG;

ARTICLE; ASPERGILLUS NIDULANS; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; HYDROGEN BOND; LIGAND BINDING; MATHEMATICAL COMPUTING; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTON NUCLEAR MAGNETIC RESONANCE; TITRIMETRY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ASPERGILLUS NIDULANS; CDC25 PHOSPHATASE; CELL CYCLE PROTEINS; HUMANS; LIGANDS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDYLPROLYL ISOMERASE; PROTEIN STRUCTURE, SECONDARY; SURFACE PLASMON RESONANCE;

EMERICELLA NIDULANS; MAMMALIA;

EID: 34548225350     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.06.006     Document Type: Article

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