2lbd

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{{STRUCTURE_2lbd| PDB=2lbd | SCENE= }}
{{STRUCTURE_2lbd| PDB=2lbd | SCENE= }}
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'''LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO ALL-TRANS RETINOIC ACID'''
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===LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO ALL-TRANS RETINOIC ACID===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 7501014 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7501014}}
==About this Structure==
==About this Structure==
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[[Category: Structural proteomics in europe]]
[[Category: Structural proteomics in europe]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:20:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:33:48 2008''

Revision as of 19:33, 27 July 2008

Image:2lbd.png

Template:STRUCTURE 2lbd

LIGAND-BINDING DOMAIN OF THE HUMAN RETINOIC ACID RECEPTOR GAMMA BOUND TO ALL-TRANS RETINOIC ACID

Template:ABSTRACT PUBMED 7501014

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

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