1mvc
From Proteopedia
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|PDB= 1mvc |SIZE=350|CAPTION= <scene name='initialview01'>1mvc</scene>, resolution 1.9Å | |PDB= 1mvc |SIZE=350|CAPTION= <scene name='initialview01'>1mvc</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BM6:4-[2-(5,5,8,8-TETRAMETHYL-5,6,7,8-TETRAHYDRO-NAPHTHALEN-2-YL)-[1,3]DIOXOLAN-2-YL]-BENZOIC ACID'>BM6</scene> | + | |LIGAND= <scene name='pdbligand=BM6:4-[2-(5,5,8,8-TETRAMETHYL-5,6,7,8-TETRAHYDRO-NAPHTHALEN-2-YL)-[1,3]DIOXOLAN-2-YL]-BENZOIC+ACID'>BM6</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fby|1FBY]], [[1mv9|1MV9]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mvc OCA], [http://www.ebi.ac.uk/pdbsum/1mvc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mvc RCSB]</span> | ||
}} | }} | ||
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[[Category: Mitschler, A.]] | [[Category: Mitschler, A.]] | ||
[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
| - | [[Category: BM6]] | ||
[[Category: agonist recognition]] | [[Category: agonist recognition]] | ||
[[Category: nuclear receptor]] | [[Category: nuclear receptor]] | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''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 22:21:38 2008'' |
Revision as of 19:21, 30 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1FBY, 1MV9
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the human RXR alpha ligand binding domain bound to the synthetic agonist compound BMS 649 and a coactivator peptide
Overview
The nuclear receptor RXR is an obligate partner in many signal transduction pathways. We report the high-resolution structures of two complexes of the human RXRalpha ligand-binding domain specifically bound to two different and chemically unrelated agonist compounds: docosa hexaenoic acid, a natural derivative of eicosanoic acid, present in mammalian cells and recently identified as a potential endogenous RXR ligand in the mouse brain, and the synthetic ligand BMS 649. In both structures the RXR-ligand-binding domain forms homodimers and exhibits the active conformation previously observed with 9-cis-RA. Analysis of the differences in ligand-protein contacts (predominantly van der Waals forces) and binding cavity geometries and volumes for the several agonist-bound RXR structures clarifies the structural features important for ligand recognition. The L-shaped ligand-binding pocket adapts to the diverse ligands, especially at the level of residue N306, which might thus constitute a new target for drug-design. Despite its highest affinity 9-cis-RA displays the lowest number of ligand-protein contacts. These structural results support the idea that docosa hexaenoic acid and related fatty acids could be natural agonists of RXRs and question the real nature of the endogenous ligand(s) in mammalian cells.
About this Structure
1MVC is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Molecular recognition of agonist ligands by RXRs., Egea PF, Mitschler A, Moras D, Mol Endocrinol. 2002 May;16(5):987-97. PMID:11981034
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