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PDBsum entry 4ozt
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Transcription
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PDB id
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4ozt
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References listed in PDB file
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Key reference
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Title
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Unprecedented conformational flexibility revealed in the ligand-Binding domains of the bovicola ovis ecdysone receptor (ecr) and ultraspiracle (usp) subunits.
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Authors
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B.Ren,
T.S.Peat,
V.A.Streltsov,
M.Pollard,
R.Fernley,
J.Grusovin,
S.Seabrook,
P.Pilling,
T.Phan,
L.Lu,
G.O.Lovrecz,
L.D.Graham,
R.J.Hill.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2014,
70,
1954-1964.
[DOI no: ]
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PubMed id
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Abstract
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The heterodimeric ligand-binding region of the Bovicola ovis ecdysone receptor
has been crystallized either in the presence of an ecdysteroid or a synthetic
methylene lactam insecticide. Two X-ray crystallographic structures, determined
at 2.7 Å resolution, show that the ligand-binding domains of both subunits of
this receptor, like those of other nuclear receptors, can display significant
conformational flexibility. Thermal melt experiments show that while ponasterone
A stabilizes the higher order structure of the heterodimer in solution, the
methylene lactam destabilizes it. The conformations of the EcR and USP subunits
observed in the structure crystallized in the presence of the methylene lactam
have not been seen previously in any ecdysone receptor structure and represent a
new level of conformational flexibility for these important receptors.
Interestingly, the new USP conformation presents an open, unoccupied
ligand-binding pocket.
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