1dkf

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(New page: 200px<br /> <applet load="1dkf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dkf, resolution 2.50&Aring;" /> '''CRYSTAL STRUCTURE O...)
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<applet load="1dkf" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1dkf, resolution 2.50&Aring;" />
caption="1dkf, resolution 2.50&Aring;" />
'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DKF OCA].
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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.]]
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[[Category: SPINE, Structural.Proteomics.in.Europe.]]
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[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: Vivat, V.]]
[[Category: Vivat, V.]]
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[[Category: Wurtz, J.M.]]
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[[Category: Wurtz, J M.]]
[[Category: BMS]]
[[Category: BMS]]
[[Category: OLA]]
[[Category: OLA]]
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[[Category: structural proteomics in europe]]
[[Category: structural proteomics in europe]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:33:23 2007''
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''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


1dkf, resolution 2.50Å

Drag the structure with the mouse to rotate

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

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