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.


2c2l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2c2l.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2c2l.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2c2l| PDB=2c2l | SCENE= }}
{{STRUCTURE_2c2l| PDB=2c2l | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE CHIP U-BOX E3 UBIQUITIN LIGASE'''
+
===CRYSTAL STRUCTURE OF THE CHIP U-BOX E3 UBIQUITIN LIGASE===
-
==Overview==
+
<!--
-
CHIP is a dimeric U box E3 ubiquitin ligase that binds Hsp90 and/or Hsp70 via its TPR-domain, facilitating ubiquitylation of chaperone bound client proteins. We have determined the crystal structure of CHIP bound to an Hsp90 C-terminal decapeptide. The structure explains how CHIP associates with either chaperone type and reveals an unusual asymmetric homodimer in which the protomers adopt radically different conformations. Additionally, we identified CHIP as a functional partner of Ubc13-Uev1a in formation of Lys63-linked polyubiquitin chains, extending CHIP's roles into ubiquitin regulation as well as targeted destruction. The structure of Ubc13-Uev1a bound to the CHIP U box domain defines the basis for selective cooperation of CHIP with specific ubiquitin-conjugating enzymes. Remarkably, the asymmetric arrangement of the TPR domains in the CHIP dimer occludes one Ubc binding site, so that CHIP operates with half-of-sites activity, providing an elegant means for coupling a dimeric chaperone to a single ubiquitylation system.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16307917}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16307917 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16307917}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Tpr]]
[[Category: Tpr]]
[[Category: Ubiquitinylation]]
[[Category: Ubiquitinylation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:09:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:18:07 2008''

Revision as of 10:18, 27 July 2008

Image:2c2l.png

Template:STRUCTURE 2c2l

CRYSTAL STRUCTURE OF THE CHIP U-BOX E3 UBIQUITIN LIGASE

Template:ABSTRACT PUBMED 16307917

About this Structure

2C2L is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex., Zhang M, Windheim M, Roe SM, Peggie M, Cohen P, Prodromou C, Pearl LH, Mol Cell. 2005 Nov 23;20(4):525-38. PMID:16307917

Page seeded by OCA on Sun Jul 27 13:18:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c2l"
Personal tools