2c2l
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | CHIP is a dimeric U box E3 ubiquitin ligase that binds Hsp90 and/or Hsp70 | + | 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. |
==About this Structure== | ==About this Structure== | ||
| Line 13: | Line 13: | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Pearl, L | + | [[Category: Pearl, L H.]] |
| - | [[Category: Roe, S | + | [[Category: Roe, S M.]] |
[[Category: Zhang, M.]] | [[Category: Zhang, M.]] | ||
[[Category: NI]] | [[Category: NI]] | ||
| Line 23: | Line 23: | ||
[[Category: ubiquitinylation]] | [[Category: ubiquitinylation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:44:15 2008'' |
Revision as of 14:44, 21 February 2008
|
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.
About this Structure
2C2L is a Protein complex structure of sequences from Mus musculus with and as ligands. Known structural/functional Site: . 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 Thu Feb 21 16:44:15 2008
Categories: Mus musculus | Protein complex | Pearl, L H. | Roe, S M. | Zhang, M. | NI | SO4 | E3 ligase | Heat-shock protein complex | Tpr | Ubiquitinylation
