1hg4
From Proteopedia
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==Overview== | ==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 ... | + | 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 inactive conformation. It also shows that USP has a, large hydrophobic cavity, implying that there is almost certainly a, natural ligand for USP. This cavity is larger than that seen previously, for most other nuclear receptors. Intriguingly, this cavity has partial, occupancy by a bound lipid, which is likely to resemble the natural ligand, for USP. |
==About this Structure== | ==About this Structure== | ||
| - | 1HG4 is a | + | 1HG4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with LPP as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Sites: LP1, LP2, LP3, LP4, LP5 and LP6. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HG4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:31:38 2007'' |
Revision as of 10:26, 5 November 2007
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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 inactive conformation. It also shows that USP has a, large hydrophobic cavity, implying that there is almost certainly a, natural ligand for USP. This cavity is larger than that seen previously, for most other nuclear receptors. Intriguingly, this cavity has partial, occupancy by a bound lipid, which is likely to resemble the natural ligand, for USP.
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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