1fby: Difference between revisions
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[[Image:1fby.gif|left|200px]] | [[Image:1fby.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE HUMAN RXR ALPHA LIGAND BINDING DOMAIN BOUND TO 9-CIS RETINOIC ACID''' | {{Structure | ||
|PDB= 1fby |SIZE=350|CAPTION= <scene name='initialview01'>1fby</scene>, resolution 2.25Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=REA:RETINOIC ACID'>REA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE HUMAN RXR ALPHA LIGAND BINDING DOMAIN BOUND TO 9-CIS RETINOIC ACID''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FBY is a [ | 1FBY is a [[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=1FBY OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10835357 10835357] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: retinoid receptor]] | [[Category: retinoid receptor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:07:08 2008'' | ||
Revision as of 12:07, 20 March 2008
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CRYSTAL STRUCTURE OF THE HUMAN RXR ALPHA LIGAND BINDING DOMAIN BOUND TO 9-CIS RETINOIC ACID
OverviewOverview
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 StructureAbout this Structure
1FBY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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