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.


2bj4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2bj4.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2bj4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2bj4| PDB=2bj4 | SCENE= }}
{{STRUCTURE_2bj4| PDB=2bj4 | SCENE= }}
-
'''ESTROGEN RECEPTOR ALPHA LBD IN COMPLEX WITH A PHAGE-DISPLAY DERIVED PEPTIDE ANTAGONIST'''
+
===ESTROGEN RECEPTOR ALPHA LBD IN COMPLEX WITH A PHAGE-DISPLAY DERIVED PEPTIDE ANTAGONIST===
-
==Overview==
+
<!--
-
Recent studies have identified a series of estrogen receptor (ER)-interacting peptides that recognize sites that are distinct from the classic coregulator recruitment (AF2) region. Here, we report the structural and functional characterization of an ERalpha-specific peptide that binds to the liganded receptor in an AF2-independent manner. The 2-A crystal structure of the ER/peptide complex reveals a binding site that is centered on a shallow depression on the beta-hairpin face of the ligand-binding domain. The peptide binds in an unusual extended conformation and makes multiple contacts with the ligand-binding domain. The location and architecture of the binding site provides an insight into the peptide's ER subtype specificity and ligand interaction preferences. In vivo, an engineered coactivator containing the peptide motif is able to strongly enhance the transcriptional activity of liganded ERalpha, particularly in the presence of 4-hydroxytamoxifen. Furthermore, disruption of this binding surface alters ER's response to the coregulator TIF2. Together, these results indicate that this previously unknown interaction site represents a bona fide control surface involved in regulating receptor activity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15728727}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15728727 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15728727}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Steroid-binding]]
[[Category: Steroid-binding]]
[[Category: Transcription factor]]
[[Category: Transcription factor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:21:47 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:34:58 2008''

Revision as of 13:35, 27 July 2008

Image:2bj4.png

Template:STRUCTURE 2bj4

ESTROGEN RECEPTOR ALPHA LBD IN COMPLEX WITH A PHAGE-DISPLAY DERIVED PEPTIDE ANTAGONIST

Template:ABSTRACT PUBMED 15728727

About this Structure

2BJ4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Delineation of a unique protein-protein interaction site on the surface of the estrogen receptor., Kong EH, Heldring N, Gustafsson JA, Treuter E, Hubbard RE, Pike AC, Proc Natl Acad Sci U S A. 2005 Mar 8;102(10):3593-8. Epub 2005 Feb 23. PMID:15728727

Page seeded by OCA on Sun Jul 27 16:34:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bj4"
Personal tools