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.


1t65

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1t65.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1t65.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1t65| PDB=1t65 | SCENE= }}
{{STRUCTURE_1t65| PDB=1t65 | SCENE= }}
-
'''Crystal structure of the androgen receptor ligand binding domain with DHT and a peptide derived form its physiological coactivator GRIP1 NR box 2 bound in a non-helical conformation'''
+
===Crystal structure of the androgen receptor ligand binding domain with DHT and a peptide derived form its physiological coactivator GRIP1 NR box 2 bound in a non-helical conformation===
-
==Overview==
+
<!--
-
Androgens drive sex differentiation, bone and muscle development, and promote growth of hormone-dependent cancers by binding the nuclear androgen receptor (AR), which recruits coactivators to responsive genes. Most nuclear receptors recruit steroid receptor coactivators (SRCs) to their ligand binding domain (LBD) using a leucine-rich motif (LXXLL). AR is believed to recruit unique coactivators to its LBD using an aromatic-rich motif (FXXLF) while recruiting SRCs to its N-terminal domain (NTD) through an alternate mechanism. Here, we report that the AR-LBD interacts with both FXXLF motifs and a subset of LXXLL motifs and that contacts with these LXXLL motifs are both necessary and sufficient for SRC-mediated AR regulation of transcription. Crystal structures of the activated AR in complex with both recruitment motifs reveal that side chains unique to the AR-LBD rearrange to bind either the bulky FXXLF motifs or the more compact LXXLL motifs and that AR utilizes subsidiary contacts with LXXLL flanking sequences to discriminate between LXXLL motifs.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15563469}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15563469 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15563469}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Webb, P.]]
[[Category: Webb, P.]]
[[Category: Androgen receptor ligand binding domain grip1 nr box2 coactivators crystal structure non-helical]]
[[Category: Androgen receptor ligand binding domain grip1 nr box2 coactivators crystal structure non-helical]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:34:36 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:12:19 2008''

Revision as of 14:12, 27 July 2008

Template:STRUCTURE 1t65

Crystal structure of the androgen receptor ligand binding domain with DHT and a peptide derived form its physiological coactivator GRIP1 NR box 2 bound in a non-helical conformation

Template:ABSTRACT PUBMED 15563469

About this Structure

1T65 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The molecular mechanisms of coactivator utilization in ligand-dependent transactivation by the androgen receptor., Estebanez-Perpina E, Moore JM, Mar E, Delgado-Rodrigues E, Nguyen P, Baxter JD, Buehrer BM, Webb P, Fletterick RJ, Guy RK, J Biol Chem. 2005 Mar 4;280(9):8060-8. Epub 2004 Nov 24. PMID:15563469

Page seeded by OCA on Sun Jul 27 17:12:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools