2lbd: Difference between revisions
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[[Image:2lbd.jpg|left|200px]] | [[Image:2lbd.jpg|left|200px]] | ||
'''LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO ALL-TRANS RETINOIC ACID''' | {{Structure | ||
|PDB= 2lbd |SIZE=350|CAPTION= <scene name='initialview01'>2lbd</scene>, resolution 2.06Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=REA:RETINOIC ACID'>REA</scene> | |||
|ACTIVITY= | |||
|GENE= HUMAN RAR GAMMA A CDNA (NUCLEOTIDES 946 - 1683) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO ALL-TRANS RETINOIC ACID''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2LBD is a [ | 2LBD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LBD OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid., Renaud JP, Rochel N, Ruff M, Vivat V, Chambon P, Gronemeyer H, Moras D, Nature. 1995 Dec 14;378(6558):681-9. PMID:[http:// | Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid., Renaud JP, Rochel N, Ruff M, Vivat V, Chambon P, Gronemeyer H, Moras D, Nature. 1995 Dec 14;378(6558):681-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7501014 7501014] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: retinoic acid receptor]] | [[Category: retinoic acid receptor]] | ||
[[Category: spine]] | [[Category: spine]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:46:33 2008'' | ||
Revision as of 15:46, 20 March 2008
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| 2lbd, resolution 2.06Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | REA | ||||||||||||
| Gene: | HUMAN RAR GAMMA A CDNA (NUCLEOTIDES 946 - 1683) (Homo sapiens) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO ALL-TRANS RETINOIC ACID
Overview
The 2.0-A crystal structure of the ligand-binding domain (LBD) of the human retinoic acid receptor (RAR)-gamma bound to all-trans retinoic acid reveals the ligand-binding interactions and suggests an electrostatic guidance mechanism. The overall fold is similar to that of the human RXR-alpha apo-LBD, except for the carboxy-terminal part which folds back towards the LBD core, contributing to the hydrophobic ligand pocket and 'sealing' its entry site. We propose a 'mouse trap' mechanism whereby a ligand-induced conformational transition repositions the amphipathic alpha-helix of the AF-2 activating domain and forms a transcriptionally active receptor.
About this Structure
2LBD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid., Renaud JP, Rochel N, Ruff M, Vivat V, Chambon P, Gronemeyer H, Moras D, Nature. 1995 Dec 14;378(6558):681-9. PMID:7501014
Page seeded by OCA on Thu Mar 20 17:46:33 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Homo sapiens
- Single protein
- Moras, D.
- Renaud, J P.
- Rochel, N.
- Ruff, M.
- SPINE, Structural Proteomics in Europe.
- REA
- Active conformation
- All-trans retinoic acid
- Complex
- Holo form
- Ligand-binding domain
- Ligand-dependent
- Nuclear receptor
- Retinoic acid receptor
- Spine
- Structural genomic
- Structural proteomics in europe
- Transcription regulation
