1hg4
From Proteopedia
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ULTRASPIRACLE LIGAND BINDING DOMAIN FROM DROSOPHILA MELANOGASTER
Overview
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 Structure
1HG4 is a [Single protein] structure of sequence from [Drosophila melanogaster] with LPP as [ligand]. Structure known Active Sites: LP1, LP2, LP3, LP4, LP5 and LP6. Full crystallographic information is available from [OCA].
Reference
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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