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TitleUnprecedented conformational flexibility revealed in the ligand-binding domains of the Bovicola ovis ecdysone receptor (EcR) and ultraspiracle (USP) subunits.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 70, Page 1954-1964, Year 2014
Publish dateFeb 18, 2014 (structure data deposition date)
AuthorsRen, B. / Peat, T.S. / Streltsov, V.A. / Pollard, M. / Fernley, R. / Grusovin, J. / Seabrook, S. / Pilling, P. / Phan, T. / Lu, L. ...Ren, B. / Peat, T.S. / Streltsov, V.A. / Pollard, M. / Fernley, R. / Grusovin, J. / Seabrook, S. / Pilling, P. / Phan, T. / Lu, L. / Lovrecz, G.O. / Graham, L.D. / Hill, R.J.
External linksActa Crystallogr. ,Sect. D / PubMed:25004972
MethodsX-ray diffraction
Resolution2.7 Å
Structure data

PDB-4ozr:
Crystal structure of the ligand binding domains of the Bovicola ovis ecdysone receptor EcR/USP heterodimer (methylene lactam crystal)
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-4ozt:
crystal structure of the ligand binding domains of the Bovicola ovis ecdysone receptor EcR/USP heterodimer (PonA crystal)
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-P1A:
2,3,14,20,22-PENTAHYDROXYCHOLEST-7-EN-6-ONE

ChemComp-NEQ:
N-ETHYLMALEIMIDE

Source
  • pediculus humanus subsp. corporis (human body louse)
KeywordsTRANSCRIPTION / Ecdysone receptor / USP / methylene lactam / heterodimer / ligand binding domain / PonA

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