1dkf: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1dkf |SIZE=350|CAPTION= <scene name='initialview01'>1dkf</scene>, resolution 2.50Å | |PDB= 1dkf |SIZE=350|CAPTION= <scene name='initialview01'>1dkf</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=BMS:4-[(4,4-DIMETHYL-1,2,3,4-TETRAHYDRO-[1,2']BINAPTHALENYL-7-CARBONYL)-AMINO]-BENZOIC+ACID'>BMS</scene> | |LIGAND= <scene name='pdbligand=BMS:4-[(4,4-DIMETHYL-1,2,3,4-TETRAHYDRO-[1,2']BINAPTHALENYL-7-CARBONYL)-AMINO]-BENZOIC+ACID'>BMS</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1lbd|1LBD]], [[2lbd|2LBD]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dkf OCA], [http://www.ebi.ac.uk/pdbsum/1dkf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dkf RCSB]</span> | |||
}} | }} | ||
| Line 14: | Line 17: | ||
==Overview== | ==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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
| Line 33: | Line 33: | ||
[[Category: Vivat, V.]] | [[Category: Vivat, V.]] | ||
[[Category: Wurtz, J M.]] | [[Category: Wurtz, J M.]] | ||
[[Category: helical sandwich]] | [[Category: helical sandwich]] | ||
[[Category: heterodimer]] | [[Category: heterodimer]] | ||
| Line 43: | Line 41: | ||
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:43:16 2008'' | ||
Revision as of 16:43, 30 March 2008
| |||||||||||||
| 1dkf, resolution 2.50Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | BMS, OLA | ||||||||||||
| Related: | 1LBD, 2LBD
| ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF A HETERODIMERIC COMPLEX OF RAR AND RXR LIGAND-BINDING DOMAINS
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.
About this Structure
1DKF is a Protein complex structure of sequences from Homo sapiens and Mus musculus. 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 Sun Mar 30 19:43:16 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Homo sapiens
- Mus musculus
- Protein complex
- Bourguet, W.
- Chambon, P.
- Gronemeyer, H.
- Moras, D.
- SPINE, Structural Proteomics in Europe.
- Vivat, V.
- Wurtz, J M.
- Helical sandwich
- Heterodimer
- Hormone/growth factor receptor
- Protein-ligand complex
- Spine
- Structural genomic
- Structural proteomics in europe
