1fby

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[[Image:1fby.gif|left|200px]]
[[Image:1fby.gif|left|200px]]
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{{Structure
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|PDB= 1fby |SIZE=350|CAPTION= <scene name='initialview01'>1fby</scene>, resolution 2.25&Aring;
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The line below this paragraph, containing "STRUCTURE_1fby", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=REA:RETINOIC+ACID'>REA</scene>
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{{STRUCTURE_1fby| PDB=1fby | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fby OCA], [http://www.ebi.ac.uk/pdbsum/1fby PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fby RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF THE HUMAN RXR ALPHA LIGAND BINDING DOMAIN BOUND TO 9-CIS RETINOIC ACID'''
'''CRYSTAL STRUCTURE OF THE HUMAN RXR ALPHA LIGAND BINDING DOMAIN BOUND TO 9-CIS RETINOIC ACID'''
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[[Category: Rochel, N.]]
[[Category: Rochel, N.]]
[[Category: Ruff, M.]]
[[Category: Ruff, M.]]
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[[Category: nuclear receptor]]
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[[Category: Nuclear receptor]]
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[[Category: protein-ligand complex]]
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[[Category: Protein-ligand complex]]
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[[Category: retinoid receptor]]
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[[Category: Retinoid receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:08:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:19:54 2008''
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Revision as of 13:08, 2 May 2008

Template:STRUCTURE 1fby

CRYSTAL STRUCTURE OF THE HUMAN RXR ALPHA LIGAND BINDING DOMAIN BOUND TO 9-CIS RETINOIC ACID


Overview

The pleiotropic effects of active retinoids are transduced by their cognate nuclear receptors, retinoid X receptors (RXRs) and retinoic acid receptors (RARs), which act as transcriptional regulators activated by two stereoisomers of retinoic acid (RA): 9-cis RA (9-cRA) and all-trans RA (a-tRA). Among nuclear receptors, RXR occupies a central position and plays a crucial role in many intracellular signalling pathways as a ubiquitous heterodimerization partner with numerous other members of this superfamily. Whereas RARs bind both isomers, RXRs exclusively bind 9-cRA. The crystal structure of the ligand-binding domain (LBD) of human RXRalpha bound to 9-cRA reveals the molecular basis of this ligand selectivity and allows a comparison of both apo and holo forms of the same nuclear receptor. In the crystal, the receptor is monomeric and exhibits a canonical agonist conformation without direct contacts between the ligand and the transactivation helix H12. Comparison with the unliganded RXRalpha LBD structure reveals the molecular mechanisms of ligand-induced conformational changes and allows us to describe at the atomic level how these changes generate the proper protein interface involved in nuclear receptor-coactivator interaction.

About this Structure

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

Reference

Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid., Egea PF, Mitschler A, Rochel N, Ruff M, Chambon P, Moras D, EMBO J. 2000 Jun 1;19(11):2592-601. PMID:10835357 Page seeded by OCA on Fri May 2 16:08:57 2008

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