2lbd
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LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO ALL-TRANS RETINOIC ACID
OverviewOverview
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 StructureAbout this Structure
2LBD is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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 Fri Feb 15 17:37:32 2008
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- 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 genomics
- Structural proteomics in europe
- Transcription regulation