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'''Crystal Structure of the Ligand-Binding Domains of the T.castaneum (Coleoptera) Heterodimer EcrUSP Bound to Ponasterone A''' | '''Crystal Structure of the Ligand-Binding Domains of the T.castaneum (Coleoptera) Heterodimer EcrUSP Bound to Ponasterone A''' | ||
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==About this Structure== | ==About this Structure== | ||
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NXX OCA]. | |||
==Reference== | ==Reference== | ||
Structural and functional characterization of a novel type of ligand-independent RXR-USP receptor., Iwema T, Billas IM, Beck Y, Bonneton F, Nierengarten H, Chaumot A, Richards G, Laudet V, Moras D, EMBO J. 2007 Aug 22;26(16):3770-82. Epub 2007 Aug 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17673910 17673910] | Structural and functional characterization of a novel type of ligand-independent RXR-USP receptor., Iwema T, Billas IM, Beck Y, Bonneton F, Nierengarten H, Chaumot A, Richards G, Laudet V, Moras D, EMBO J. 2007 Aug 22;26(16):3770-82. Epub 2007 Aug 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17673910 17673910] | ||
[[Category: Billas, I.]] | [[Category: Billas, I.]] | ||
[[Category: Iwema, T.]] | [[Category: Iwema, T.]] | ||
[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
[[Category: | [[Category: Apo and holo ligand binding pocket]] | ||
[[Category: | [[Category: Hormone receptor]] | ||
[[Category: | [[Category: Hormone/growth factor complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 10:03:11 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 07:03, 4 May 2008
Crystal Structure of the Ligand-Binding Domains of the T.castaneum (Coleoptera) Heterodimer EcrUSP Bound to Ponasterone A
Overview
Retinoid X receptor (RXR) and Ultraspiracle (USP) play a central role as ubiquitous heterodimerization partners of many nuclear receptors. While it has long been accepted that a wide range of ligands can activate vertebrate/mollusc RXRs, the existence and necessity of specific endogenous ligands activating RXR-USP in vivo is still matter of intense debate. Here we report the existence of a novel type of RXR-USP with a ligand-independent functional conformation. Our studies involved Tribolium USP (TcUSP) as representative of most arthropod RXR-USPs, with high sequence homology to vertebrate/mollusc RXRs. The crystal structure of the ligand-binding domain of TcUSP was solved in the context of the functional heterodimer with the ecdysone receptor (EcR). While EcR exhibits a canonical ligand-bound conformation, USP adopts an original apo structure. Our functional data demonstrate that TcUSP is a constitutively silent partner of EcR, and that none of the RXR ligands can bind and activate TcUSP. These findings together with a phylogenetic analysis suggest that RXR-USPs have undergone remarkable functional shifts during evolution and give insight into receptor-ligand binding evolution and dynamics.
About this Structure
Full crystallographic information is available from OCA.
Reference
Structural and functional characterization of a novel type of ligand-independent RXR-USP receptor., Iwema T, Billas IM, Beck Y, Bonneton F, Nierengarten H, Chaumot A, Richards G, Laudet V, Moras D, EMBO J. 2007 Aug 22;26(16):3770-82. Epub 2007 Aug 2. PMID:17673910 Page seeded by OCA on Sun May 4 10:03:11 2008
