1hg4

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[[Image:1hg4.gif|left|200px]]<br /><applet load="1hg4" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hg4.gif|left|200px]]
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caption="1hg4, resolution 2.4&Aring;" />
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'''ULTRASPIRACLE LIGAND BINDING DOMAIN FROM DROSOPHILA MELANOGASTER'''<br />
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{{Structure
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|PDB= 1hg4 |SIZE=350|CAPTION= <scene name='initialview01'>1hg4</scene>, resolution 2.4&Aring;
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|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>
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|LIGAND= <scene name='pdbligand=LPP:2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE'>LPP</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''ULTRASPIRACLE LIGAND BINDING DOMAIN FROM DROSOPHILA MELANOGASTER'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=LPP:'>LPP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HG4 OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11171988 11171988]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:00:55 2008''
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''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


PDB ID 1hg4

Drag the structure with the mouse to rotate
, resolution 2.4Å
Sites: , , , , and
Ligands:
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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