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2lbd
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The 2.0-A crystal structure of the ligand-binding domain (LBD) of the | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
| - | [[Category: Renaud, J | + | [[Category: Renaud, J P.]] |
[[Category: Rochel, N.]] | [[Category: Rochel, N.]] | ||
[[Category: Ruff, M.]] | [[Category: Ruff, M.]] | ||
| - | [[Category: SPINE, Structural | + | [[Category: SPINE, Structural Proteomics in Europe.]] |
[[Category: REA]] | [[Category: REA]] | ||
[[Category: active conformation]] | [[Category: active conformation]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:06:59 2008'' |
Revision as of 16:07, 21 February 2008
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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 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 Thu Feb 21 18:06:59 2008
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
