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1dkf
From Proteopedia
(New page: 200px<br /> <applet load="1dkf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dkf, resolution 2.50Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:1dkf.gif|left|200px]]<br /> | + | [[Image:1dkf.gif|left|200px]]<br /><applet load="1dkf" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1dkf" size=" | + | |
caption="1dkf, resolution 2.50Å" /> | caption="1dkf, resolution 2.50Å" /> | ||
'''CRYSTAL STRUCTURE OF A HETERODIMERIC COMPLEX OF RAR AND RXR LIGAND-BINDING DOMAINS'''<br /> | '''CRYSTAL STRUCTURE OF A HETERODIMERIC COMPLEX OF RAR AND RXR LIGAND-BINDING DOMAINS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of a heterodimer between the ligand-binding domains | + | The crystal structure of a heterodimer between the ligand-binding domains (LBDs) of the human RARalpha bound to a selective antagonist and the constitutively active mouse RXRalphaF318A mutant shows that, pushed by a bulky extension of the ligand, RARalpha helix H12 adopts an antagonist position. The unexpected presence of a fatty acid in the ligand-binding pocket of RXRalpha(F318A is likely to account for its apparent "constitutivity." Specific conformational changes suggest the structural basis of pure and partial antagonism. The RAR-RXR heterodimer interface is similar to that observed in most nuclear receptor (NR) homodimers. A correlative analysis of 3D structures and sequences provides a novel view on dimerization among members of the nuclear receptor superfamily. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DKF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with BMS and OLA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1DKF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=BMS:'>BMS</scene> and <scene name='pdbligand=OLA:'>OLA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DKF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gronemeyer, H.]] | [[Category: Gronemeyer, H.]] | ||
[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
| - | [[Category: SPINE, Structural | + | [[Category: SPINE, Structural Proteomics in Europe.]] |
[[Category: Vivat, V.]] | [[Category: Vivat, V.]] | ||
| - | [[Category: Wurtz, J | + | [[Category: Wurtz, J M.]] |
[[Category: BMS]] | [[Category: BMS]] | ||
[[Category: OLA]] | [[Category: OLA]] | ||
| Line 35: | Line 34: | ||
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:29 2008'' |
Revision as of 10:17, 21 February 2008
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CRYSTAL STRUCTURE OF A HETERODIMERIC COMPLEX OF RAR AND RXR LIGAND-BINDING DOMAINS
Contents |
Overview
The crystal structure of a heterodimer between the ligand-binding domains (LBDs) of the human RARalpha bound to a selective antagonist and the constitutively active mouse RXRalphaF318A mutant shows that, pushed by a bulky extension of the ligand, RARalpha helix H12 adopts an antagonist position. The unexpected presence of a fatty acid in the ligand-binding pocket of RXRalpha(F318A is likely to account for its apparent "constitutivity." Specific conformational changes suggest the structural basis of pure and partial antagonism. The RAR-RXR heterodimer interface is similar to that observed in most nuclear receptor (NR) homodimers. A correlative analysis of 3D structures and sequences provides a novel view on dimerization among members of the nuclear receptor superfamily.
Disease
Known disease associated with this structure: Leukemia, acute promyelocytic OMIM:[180240]
About this Structure
1DKF is a Protein complex structure of sequences from Homo sapiens and Mus musculus with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains., Bourguet W, Vivat V, Wurtz JM, Chambon P, Gronemeyer H, Moras D, Mol Cell. 2000 Feb;5(2):289-98. PMID:10882070
Page seeded by OCA on Thu Feb 21 12:17:29 2008
Categories: Homo sapiens | Mus musculus | Protein complex | Bourguet, W. | Chambon, P. | Gronemeyer, H. | Moras, D. | SPINE, Structural Proteomics in Europe. | Vivat, V. | Wurtz, J M. | BMS | OLA | Helical sandwich | Heterodimer | Hormone/growth factor receptor | Protein-ligand complex | Spine | Structural genomics | Structural proteomics in europe
