1hg4

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[[Image:1hg4.gif|left|200px]]<br /><applet load="1hg4" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hg4.gif|left|200px]]<br /><applet load="1hg4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1hg4, resolution 2.4&Aring;" />
caption="1hg4, resolution 2.4&Aring;" />
'''ULTRASPIRACLE LIGAND BINDING DOMAIN FROM DROSOPHILA MELANOGASTER'''<br />
'''ULTRASPIRACLE LIGAND BINDING DOMAIN FROM DROSOPHILA MELANOGASTER'''<br />
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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 LPP 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HG4 OCA].
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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].
==Reference==
==Reference==
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[[Category: transcription factor]]
[[Category: transcription factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:22:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:49:10 2008''

Revision as of 07:49, 3 February 2008


1hg4, resolution 2.4Å

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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 as ligand. Known structural/functional Sites: , , , , and . 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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