2lbd
From Proteopedia
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 Sun Apr 13 08:20:34 2008
Categories: Homo sapiens | Single protein | Moras, D. | Renaud, J P. | Rochel, N. | Ruff, M. | SPINE, Structural Proteomics in Europe. | 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
