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2lbd
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(New page: 200px<br /> <applet load="2lbd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2lbd, resolution 2.06Å" /> '''LIGAND-BINDING DOMA...)
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Revision as of 20:51, 12 November 2007
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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
Page seeded by OCA on Mon Nov 12 22:58:12 2007
Categories: 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
