1hg4

Revision as of 17:03, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1hg4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hg4, resolution 2.4Å" /> '''ULTRASPIRACLE LIGAND...)
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ULTRASPIRACLE LIGAND BINDING DOMAIN FROM DROSOPHILA MELANOGASTER

File:1hg4.gif


1hg4, resolution 2.4Å

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OverviewOverview

Ultraspiracle (USP) is the invertebrate homologue of the mammalian, retinoid X receptor (RXR). RXR plays a uniquely important role in, differentiation, development, and homeostasis through its ability to serve, as a heterodimeric partner to many other nuclear receptors. RXR is able to, influence the activity of its partner receptors through the action of the, ligand 9-cis retinoic acid. In contrast to RXR, USP has no known, high-affinity ligand and is thought to be a silent component in the, heterodimeric complex with partner receptors such as the ecdysone, receptor. Here we report the 2.4-A crystal structure of the USP, ligand-binding domain. The structure shows that a conserved sequence motif, found in dipteran and lepidopteran USPs, but not in mammalian RXRs, serves, to lock USP in an ... [(full description)]

About this StructureAbout this Structure

1HG4 is a [Single protein] structure of sequence from [Drosophila melanogaster] with LPP as [ligand]. Full crystallographic information is available from [OCA].

ReferenceReference

The structure of the ultraspiracle ligand-binding domain reveals a nuclear receptor locked in an inactive conformation., Clayton GM, Peak-Chew SY, Evans RM, Schwabe JW, Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1549-54. Epub 2001 Feb 6. PMID:11171988

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