1hg4
From Proteopedia
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|PDB= 1hg4 |SIZE=350|CAPTION= <scene name='initialview01'>1hg4</scene>, resolution 2.4Å | |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> | |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> | + | |LIGAND= <scene name='pdbligand=LPP:2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL+HEXADECANOATE'>LPP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hg4 OCA], [http://www.ebi.ac.uk/pdbsum/1hg4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hg4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Clayton, G M.]] | [[Category: Clayton, G M.]] | ||
[[Category: Schwabe, J W.R.]] | [[Category: Schwabe, J W.R.]] | ||
| - | [[Category: LPP]] | ||
[[Category: ligand binding]] | [[Category: ligand binding]] | ||
[[Category: nuclear hormone receptor]] | [[Category: nuclear hormone receptor]] | ||
[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:04:22 2008'' |
Revision as of 18:04, 30 March 2008
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| , resolution 2.4Å | |||||||
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| Sites: | , , , , and | ||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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