1lbd: Difference between revisions

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New page: left|200px<br /> <applet load="1lbd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lbd, resolution 2.7Å" /> '''LIGAND-BINDING DOMAI...
 
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[[Image:1lbd.gif|left|200px]]<br />
[[Image:1lbd.gif|left|200px]]<br /><applet load="1lbd" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1lbd" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1lbd, resolution 2.7&Aring;" />
caption="1lbd, resolution 2.7&Aring;" />
'''LIGAND-BINDING DOMAIN OF THE HUMAN NUCLEAR RECEPTOR RXR-ALPHA'''<br />
'''LIGAND-BINDING DOMAIN OF THE HUMAN NUCLEAR RECEPTOR RXR-ALPHA'''<br />


==Overview==
==Overview==
The crystal structure of the human retinoid-X receptor RXR-alpha, ligand-binding domain reveals a previously undiscovered fold of an, antiparallel alpha-helical sandwich, packed as dimeric units. Two helices, and one loop form the homodimerization surface, and hydrophobic heptad, repeats participate in stabilizing the fold. The existence of a, ligand-binding pocket is proposed that would allow 9-cis retinoic acid to, interact with different functional modules, including the AF-2 activating, domain. Several lines of evidence indicate that the overall structure is a, prototype fold of ligand-binding domains of nuclear receptors.
The crystal structure of the human retinoid-X receptor RXR-alpha ligand-binding domain reveals a previously undiscovered fold of an antiparallel alpha-helical sandwich, packed as dimeric units. Two helices and one loop form the homodimerization surface, and hydrophobic heptad repeats participate in stabilizing the fold. The existence of a ligand-binding pocket is proposed that would allow 9-cis retinoic acid to interact with different functional modules, including the AF-2 activating domain. Several lines of evidence indicate that the overall structure is a prototype fold of ligand-binding domains of nuclear receptors.


==About this Structure==
==About this Structure==
1LBD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LBD OCA].  
1LBD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBD OCA].  


==Reference==
==Reference==
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[[Category: Bourguet, W.]]
[[Category: Bourguet, W.]]
[[Category: Moras, D.]]
[[Category: Moras, D.]]
[[Category: SPINE, Structural.Proteomics.in.Europe.]]
[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: nuclear receptor]]
[[Category: nuclear receptor]]
[[Category: spine]]
[[Category: spine]]
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[[Category: transcription factor]]
[[Category: transcription factor]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:58:28 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:25 2008''

Revision as of 11:43, 21 February 2008

File:1lbd.gif


1lbd, resolution 2.7Å

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LIGAND-BINDING DOMAIN OF THE HUMAN NUCLEAR RECEPTOR RXR-ALPHA

Overview

The crystal structure of the human retinoid-X receptor RXR-alpha ligand-binding domain reveals a previously undiscovered fold of an antiparallel alpha-helical sandwich, packed as dimeric units. Two helices and one loop form the homodimerization surface, and hydrophobic heptad repeats participate in stabilizing the fold. The existence of a ligand-binding pocket is proposed that would allow 9-cis retinoic acid to interact with different functional modules, including the AF-2 activating domain. Several lines of evidence indicate that the overall structure is a prototype fold of ligand-binding domains of nuclear receptors.

About this Structure

1LBD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha., Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D, Nature. 1995 Jun 1;375(6530):377-82. PMID:7760929

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