2lbd

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spinqualitylabelsall models 2lbd, resolution 2.06Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 with REA as ligand. 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

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