1mzn
From Proteopedia
(New page: 200px<br /> <applet load="1mzn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mzn, resolution 1.90Å" /> '''CRYSTAL STRUCTURE a...) |
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caption="1mzn, resolution 1.90Å" /> | caption="1mzn, resolution 1.90Å" /> | ||
'''CRYSTAL STRUCTURE at 1.9 ANGSTROEMS RESOLUTION OF THE HOMODIMER OF HUMAN RXR ALPHA LIGAND BINDING DOMAIN BOUND TO THE SYNTHETIC AGONIST COMPOUND BMS 649 AND A COACTIVATOR PEPTIDE'''<br /> | '''CRYSTAL STRUCTURE at 1.9 ANGSTROEMS RESOLUTION OF THE HOMODIMER OF HUMAN RXR ALPHA LIGAND BINDING DOMAIN BOUND TO THE SYNTHETIC AGONIST COMPOUND BMS 649 AND A COACTIVATOR PEPTIDE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MZN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with BM6 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MZN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=BM6:'>BM6</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcription]] | [[Category: transcription]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:26:21 2008'' |
Revision as of 14:26, 15 February 2008
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CRYSTAL STRUCTURE at 1.9 ANGSTROEMS RESOLUTION OF THE HOMODIMER OF 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
1MZN is a Protein complex structure of sequences from Homo sapiens with as ligand. 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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