This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1l2i

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1l2i.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1l2i.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1l2i| PDB=1l2i | SCENE= }}
{{STRUCTURE_1l2i| PDB=1l2i | SCENE= }}
-
'''Human Estrogen Receptor alpha Ligand-binding Domain in Complex with (R,R)-5,11-cis-diethyl-5,6,11,12-tetrahydrochrysene-2,8-diol and a Glucocorticoid Receptor Interacting Protein 1 NR box II Peptide'''
+
===Human Estrogen Receptor alpha Ligand-binding Domain in Complex with (R,R)-5,11-cis-diethyl-5,6,11,12-tetrahydrochrysene-2,8-diol and a Glucocorticoid Receptor Interacting Protein 1 NR box II Peptide===
-
==Overview==
+
<!--
-
The R,R enantiomer of 5,11-cis-diethyl-5,6,11,12-tetrahydrochrysene-2,8-diol (THC) exerts opposite effects on the transcriptional activity of the two estrogen receptor (ER) subtypes, ER alpha and ER beta. THC acts as an ER alpha agonist and as an ER beta antagonist. We have determined the crystal structures of the ER alpha ligand binding domain (LBD) bound to both THC and a fragment of the transcriptional coactivator GRIP1, and the ER beta LBD bound to THC. THC stabilizes a conformation of the ER alpha LBD that permits coactivator association and a conformation of the ER beta LBD that prevents coactivator association. A comparison of the two structures, taken together with functional data, reveals that THC does not act on ER beta through the same mechanisms used by other known ER antagonists. Instead, THC antagonizes ER beta through a novel mechanism we term 'passive antagonism'.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11953755}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11953755 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11953755}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Nuclear receptor]]
[[Category: Nuclear receptor]]
[[Category: Transcription factor]]
[[Category: Transcription factor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:27:47 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:33:06 2008''

Revision as of 08:33, 2 July 2008

Image:1l2i.png

Template:STRUCTURE 1l2i

Human Estrogen Receptor alpha Ligand-binding Domain in Complex with (R,R)-5,11-cis-diethyl-5,6,11,12-tetrahydrochrysene-2,8-diol and a Glucocorticoid Receptor Interacting Protein 1 NR box II Peptide

Template:ABSTRACT PUBMED 11953755

About this Structure

1L2I is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural characterization of a subtype-selective ligand reveals a novel mode of estrogen receptor antagonism., Shiau AK, Barstad D, Radek JT, Meyers MJ, Nettles KW, Katzenellenbogen BS, Katzenellenbogen JA, Agard DA, Greene GL, Nat Struct Biol. 2002 May;9(5):359-64. PMID:11953755

Page seeded by OCA on Wed Jul 2 11:33:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1l2i"
Personal tools