1exa: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:1exa.gif|left|200px]]
{{Seed}}
[[Image:1exa.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1exa|  PDB=1exa  |  SCENE=  }}  
{{STRUCTURE_1exa|  PDB=1exa  |  SCENE=  }}  


'''ENANTIOMER DISCRIMINATION ILLUSTRATED BY CRYSTAL STRUCTURES OF THE HUMAN RETINOIC ACID RECEPTOR HRARGAMMA LIGAND BINDING DOMAIN: THE COMPLEX WITH THE ACTIVE R-ENANTIOMER BMS270394.'''
===ENANTIOMER DISCRIMINATION ILLUSTRATED BY CRYSTAL STRUCTURES OF THE HUMAN RETINOIC ACID RECEPTOR HRARGAMMA LIGAND BINDING DOMAIN: THE COMPLEX WITH THE ACTIVE R-ENANTIOMER BMS270394.===




==Overview==
<!--
The human retinoic acid receptor (hRAR) is a member of the nuclear receptor superfamily that regulates the transcription of target genes in a ligand-dependent manner. The three hRAR isotypes are targets for retinoids that are used in the treatment of various diseases, including breast cancer and skin diseases. Drug efficiency and safety depend on the pharmacological activity of enantiomers, which can differ because of the chiral environment generated by the target. We report the crystal structures of the hRARgamma ligand-binding domain bound to two enantiomers, the active BMS270394 and the inactive BMS270395, solved at 1.6 A and 1.7 A resolution, respectively. The crystal structures reveal that in both enantiomers, the hydroxyl moiety attached to the chiral center forms a hydrogen bond to the Met-272 sulfur atom, thus imposing a conformation of BMS270395 that differs significantly from that observed for BMS270394 and other known retinoids. BMS270395 adopts an energetically unfavorable conformation, accounting for its inactivity; in contrast, the conformation of BMS270394 is close to an energy minimum. Our high-resolution data allow rationalization of enantiomer discrimination by the receptor and provide a model system for the pharmacological properties of enantiomeric pairs.
The line below this paragraph, {{ABSTRACT_PUBMED_10841540}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10841540 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10841540}}


==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]
[[Category: Structural proteomics in europe]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:06:09 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:09:40 2008''

Revision as of 23:09, 30 June 2008

File:1exa.png

Template:STRUCTURE 1exa

ENANTIOMER DISCRIMINATION ILLUSTRATED BY CRYSTAL STRUCTURES OF THE HUMAN RETINOIC ACID RECEPTOR HRARGAMMA LIGAND BINDING DOMAIN: THE COMPLEX WITH THE ACTIVE R-ENANTIOMER BMS270394.

Template:ABSTRACT PUBMED 10841540

About this Structure

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

Reference

Enantiomer discrimination illustrated by high-resolution crystal structures of the human nuclear receptor hRARgamma., Klaholz BP, Mitschler A, Belema M, Zusi C, Moras D, Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6322-7. PMID:10841540

Page seeded by OCA on Tue Jul 1 02:09:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1exa&oldid=594495"