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1h9u

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(New page: 200px<br /> <applet load="1h9u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h9u, resolution 2.70&Aring;" /> '''THE STRUCTURE OF TH...)
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==About this Structure==
==About this Structure==
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1H9U is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with NI, CL and LG2 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H9U OCA]].
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1H9U is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with NI, CL and LG2 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: LGA. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H9U 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 Mon Oct 29 21:52:34 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:20:22 2007''

Revision as of 12:15, 30 October 2007

Image:1h9u.gif

1h9u, resolution 2.70Å

Drag the structure with the mouse to rotate

THE STRUCTURE OF THE HUMAN RETINOID-X-RECEPTOR BETA LIGAND BINDING DOMAIN IN COMPLEX WITH THE SPECIFIC SYNTHETIC AGONIST LG100268

Overview

Ligands that specifically target retinoid-X receptors (RXRs) are emerging, as potentially powerful therapies for cancer, diabetes, and the lowering, of circulatory cholesterol. To date, RXR has only been crystallized in the, absence of ligand or with the promiscuous ligand 9-cis retinoic acid, which also activates retinoic acid receptors. Here we present the, structure of hRXRbeta in complex with the RXR-specific agonist LG100268, (LG268). The structure clearly reveals why LG268 is specific for the RXR, ligand binding pocket and will not activate retinoic acid receptors., Intriguingly, in the crystals, the C-terminal "activation" helix, (AF-2/helix H12) is trapped in a novel position not seen in other nuclear, receptor structures such that it does not cap the ligand binding cavity., ... [(full description)]

About this Structure

1H9U is a [Single protein] structure of sequence from [Homo sapiens] with NI, CL and LG2 as [ligands]. Structure known Active Site: LGA. Full crystallographic information is available from [OCA].

Reference

The structural basis for the specificity of retinoid-X receptor-selective agonists: new insights into the role of helix H12., Love JD, Gooch JT, Benko S, Li C, Nagy L, Chatterjee VK, Evans RM, Schwabe JW, J Biol Chem. 2002 Mar 29;277(13):11385-91. Epub 2002 Jan 8. PMID:11782480

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