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Title1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides.
Journal, issue, pagesJ. Biol. Chem., Vol. 276, Page 25150-25156, Year 2001
Publish dateMar 2, 2001 (structure data deposition date)
AuthorsWintjens, R. / Wieruszeski, J.M. / Drobecq, H. / Rousselot-Pailley, P. / Buee, L. / Lippens, G. / Landrieu, I.
External linksJ. Biol. Chem. / PubMed:11313338
MethodsNMR (solution)
Structure data

PDB-1i6c:
SOLUTION STRUCTURE OF PIN1 WW DOMAIN
Method: SOLUTION NMR

PDB-1i8g:
SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH CDC25 PHOSPHOTHREONINE PEPTIDE
Method: SOLUTION NMR

PDB-1i8h:
SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH HUMAN TAU PHOSPHOTHREONINE PEPTIDE
Method: SOLUTION NMR

KeywordsISOMERASE / rotamase / nuclear protein / HYDROLASE/ISOMERASE / CELL DIVISION / HYDROLASE-ISOMERASE COMPLEX / MEMBRANE PROTEIN/ISOMERASE / CYTOSKELETON / MEMBRANE PROTEIN-ISOMERASE COMPLEX

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