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TitleProline primed helix length as a modulator of the nuclear receptor-coactivator interaction
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 135, Page 4364-4371, Year 2013
Publish dateFeb 4, 2013 (structure data deposition date)
AuthorsFuchs, S. / Nguyen, H.D. / Phan, T.T. / Burton, M.F. / Nieto, L. / de Vries-van Leeuwen, I.J. / Schmidt, A. / Goodarzifard, M. / Agten, S.M. / Rose, R. ...Fuchs, S. / Nguyen, H.D. / Phan, T.T. / Burton, M.F. / Nieto, L. / de Vries-van Leeuwen, I.J. / Schmidt, A. / Goodarzifard, M. / Agten, S.M. / Rose, R. / Ottmann, C. / Milroy, L.G. / Brunsveld, L.
External linksJ. Am. Chem. Soc. / PubMed:23437920
MethodsX-ray diffraction
Resolution2.1 - 2.3 Å
Structure data

PDB-4j24:
Estrogen Receptor in complex with proline-flanked LXXLL peptides
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-4j26:
Estrogen Receptor in complex with proline-flanked LXXLL peptides
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-EST:
ESTRADIOL / hormone*YM

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHORMONE RECEPTOR/PEPTIDE / Estrogen Receptor / Proline / LXXLL / Alpha-helix / Structure stabilization / HORMONE RECEPTOR-PEPTIDE complex

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