Unprecedented conformational flexibility revealed in the ligand-binding domains of the Bovicola ovis ecdysone receptor (EcR) and ultraspiracle (USP) subunits

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.

doi:10.1107/S1399004714009626

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 1
(a) The structure of the B. ovis ecdysone receptor LBD heterodimer in a crystal formed in the presence of PonA. PonA in the pocket of the EcR subunit is shown in stick representation. H12 is coloured violet. (b) Details of the binding of PonA (aqua-coloured backbone) within the ligand-binding pocket of the EcR subunit. A difference OMIT map is shown which is contoured at the 3.5σ level. Hydrogen-bonding interactions are shown as broken lines. The structural figures in this communication were produced using PyMOL (Schrödinger).

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 70| Part 7| July 2014| Pages 1954-1964

https://doi.org/10.1107/S1399004714009626

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