1hg4
From Proteopedia
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- | [[Image:1hg4.gif|left|200px]] | + | [[Image:1hg4.gif|left|200px]] |
- | + | ||
- | '''ULTRASPIRACLE LIGAND BINDING DOMAIN FROM DROSOPHILA MELANOGASTER''' | + | {{Structure |
+ | |PDB= 1hg4 |SIZE=350|CAPTION= <scene name='initialview01'>1hg4</scene>, resolution 2.4Å | ||
+ | |SITE= <scene name='pdbsite=LP1:Lpp+Binding+Site+For+Chain+A'>LP1</scene>, <scene name='pdbsite=LP2:Lpp+Binding+Site+For+Chain+B'>LP2</scene>, <scene name='pdbsite=LP3:Lpp+Binding+Site+For+Chain+C'>LP3</scene>, <scene name='pdbsite=LP4:Lpp+Binding+Site+For+Chain+D'>LP4</scene>, <scene name='pdbsite=LP5:Lpp+Binding+Site+For+Chain+E'>LP5</scene> and <scene name='pdbsite=LP6:Lpp+Binding+Site+For+Chain+F'>LP6</scene> | ||
+ | |LIGAND= <scene name='pdbligand=LPP:2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE'>LPP</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''ULTRASPIRACLE LIGAND BINDING DOMAIN FROM DROSOPHILA MELANOGASTER''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1HG4 is a [ | + | 1HG4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HG4 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11171988 11171988] |
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:36:42 2008'' |
Revision as of 09:36, 20 March 2008
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, resolution 2.4Å | |||||||
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Sites: | , , , , and | ||||||
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Coordinates: | save as pdb, mmCIF, xml |
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. 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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