1fby: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1fby.gif|left|200px]]
{{Seed}}
[[Image:1fby.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fby|  PDB=1fby  |  SCENE=  }}  
{{STRUCTURE_1fby|  PDB=1fby  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE HUMAN RXR ALPHA LIGAND BINDING DOMAIN BOUND TO 9-CIS RETINOIC ACID'''
===CRYSTAL STRUCTURE OF THE HUMAN RXR ALPHA LIGAND BINDING DOMAIN BOUND TO 9-CIS RETINOIC ACID===




==Overview==
<!--
The pleiotropic effects of active retinoids are transduced by their cognate nuclear receptors, retinoid X receptors (RXRs) and retinoic acid receptors (RARs), which act as transcriptional regulators activated by two stereoisomers of retinoic acid (RA): 9-cis RA (9-cRA) and all-trans RA (a-tRA). Among nuclear receptors, RXR occupies a central position and plays a crucial role in many intracellular signalling pathways as a ubiquitous heterodimerization partner with numerous other members of this superfamily. Whereas RARs bind both isomers, RXRs exclusively bind 9-cRA. The crystal structure of the ligand-binding domain (LBD) of human RXRalpha bound to 9-cRA reveals the molecular basis of this ligand selectivity and allows a comparison of both apo and holo forms of the same nuclear receptor. In the crystal, the receptor is monomeric and exhibits a canonical agonist conformation without direct contacts between the ligand and the transactivation helix H12. Comparison with the unliganded RXRalpha LBD structure reveals the molecular mechanisms of ligand-induced conformational changes and allows us to describe at the atomic level how these changes generate the proper protein interface involved in nuclear receptor-coactivator interaction.
The line below this paragraph, {{ABSTRACT_PUBMED_10835357}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10835357 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10835357}}


==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Protein-ligand complex]]
[[Category: Protein-ligand complex]]
[[Category: Retinoid receptor]]
[[Category: Retinoid receptor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:08:57 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:01:16 2008''

Revision as of 00:01, 1 July 2008

File:1fby.png

Template:STRUCTURE 1fby

CRYSTAL STRUCTURE OF THE HUMAN RXR ALPHA LIGAND BINDING DOMAIN BOUND TO 9-CIS RETINOIC ACID

Template:ABSTRACT PUBMED 10835357

About this Structure

1FBY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid., Egea PF, Mitschler A, Rochel N, Ruff M, Chambon P, Moras D, EMBO J. 2000 Jun 1;19(11):2592-601. PMID:10835357

Page seeded by OCA on Tue Jul 1 03:01:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1fby&oldid=596537"