2LBD
LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO ALL-TRANS RETINOIC ACID
Summary for 2LBD
| Entry DOI | 10.2210/pdb2lbd/pdb |
| Descriptor | RETINOIC ACID RECEPTOR GAMMA, RETINOIC ACID (3 entities in total) |
| Functional Keywords | nuclear receptor, retinoic acid receptor, all-trans retinoic acid, ligand-binding domain, complex, holo form, transcription regulation, ligand-dependent, active conformation, structural proteomics in europe, spine, structural genomics |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 30493.49 |
| Authors | Renaud, J.-P.,Rochel, N.,Ruff, M.,Moras, D.,Structural Proteomics in Europe (SPINE) (deposition date: 1997-08-19, release date: 1997-11-12, Last modification date: 2024-02-21) |
| Primary citation | Renaud, J.P.,Rochel, N.,Ruff, M.,Vivat, V.,Chambon, P.,Gronemeyer, H.,Moras, D. Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid. Nature, 378:681-689, 1995 Cited by PubMed Abstract: 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. PubMed: 7501014DOI: 10.1038/378681a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.06 Å) |
Structure validation
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