1fby: Difference between revisions
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|PDB= 1fby |SIZE=350|CAPTION= <scene name='initialview01'>1fby</scene>, resolution 2.25Å | |PDB= 1fby |SIZE=350|CAPTION= <scene name='initialview01'>1fby</scene>, resolution 2.25Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=REA:RETINOIC ACID'>REA</scene> | |LIGAND= <scene name='pdbligand=REA:RETINOIC+ACID'>REA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|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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[[Category: Rochel, N.]] | [[Category: Rochel, N.]] | ||
[[Category: Ruff, M.]] | [[Category: Ruff, M.]] | ||
[[Category: nuclear receptor]] | [[Category: nuclear receptor]] | ||
[[Category: protein-ligand complex]] | [[Category: protein-ligand complex]] | ||
[[Category: retinoid receptor]] | [[Category: retinoid receptor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:19:54 2008'' | ||
Revision as of 17:19, 30 March 2008
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| 1fby, resolution 2.25Å | |||||||||||||
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| Ligands: | REA | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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