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.


1qkn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qkn.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1qkn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qkn| PDB=1qkn | SCENE= }}
{{STRUCTURE_1qkn| PDB=1qkn | SCENE= }}
-
'''RAT OESTROGEN RECEPTOR BETA LIGAND-BINDING DOMAIN IN COMPLEX WITH ANTAGONIST RALOXIFENE'''
+
===RAT OESTROGEN RECEPTOR BETA LIGAND-BINDING DOMAIN IN COMPLEX WITH ANTAGONIST RALOXIFENE===
-
==Overview==
+
<!--
-
Oestrogens exert their physiological effects through two receptor subtypes. Here we report the three-dimensional structure of the oestrogen receptor beta isoform (ERbeta) ligand-binding domain (LBD) in the presence of the phyto-oestrogen genistein and the antagonist raloxifene. The overall structure of ERbeta-LBD is very similar to that previously reported for ERalpha. Each ligand interacts with a unique set of residues within the hormone-binding cavity and induces a distinct orientation in the AF-2 helix (H12). The bulky side chain of raloxifene protrudes from the cavity and physically prevents the alignment of H12 over the bound ligand. In contrast, genistein is completely buried within the hydrophobic core of the protein and binds in a manner similar to that observed for ER's endogenous hormone, 17beta-oestradiol. However, in the ERbeta-genistein complex, H12 does not adopt the distinctive 'agonist' position but, instead, lies in a similar orientation to that induced by ER antagonists. Such a sub-optimal alignment of the transactivation helix is consistent with genistein's partial agonist character in ERbeta and demonstrates how ER's transcriptional response to certain bound ligands is attenuated.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10469641}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10469641 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10469641}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Nuclear receptor]]
[[Category: Nuclear receptor]]
[[Category: Transcription factor]]
[[Category: Transcription factor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:23:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:43:38 2008''

Revision as of 17:43, 28 July 2008

Image:1qkn.png

Template:STRUCTURE 1qkn

RAT OESTROGEN RECEPTOR BETA LIGAND-BINDING DOMAIN IN COMPLEX WITH ANTAGONIST RALOXIFENE

Template:ABSTRACT PUBMED 10469641

About this Structure

1QKN is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structure of the ligand-binding domain of oestrogen receptor beta in the presence of a partial agonist and a full antagonist., Pike AC, Brzozowski AM, Hubbard RE, Bonn T, Thorsell AG, Engstrom O, Ljunggren J, Gustafsson JA, Carlquist M, EMBO J. 1999 Sep 1;18(17):4608-18. PMID:10469641

Page seeded by OCA on Mon Jul 28 20:43:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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