2c2l: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2c2l.gif|left|200px]]<br /><applet load="2c2l" size=" | [[Image:2c2l.gif|left|200px]]<br /><applet load="2c2l" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2c2l, resolution 3.30Å" /> | caption="2c2l, resolution 3.30Å" /> | ||
'''CRYSTAL STRUCTURE OF THE CHIP U-BOX E3 UBIQUITIN LIGASE'''<br /> | '''CRYSTAL STRUCTURE OF THE CHIP U-BOX E3 UBIQUITIN LIGASE'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
2C2L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4 and NI as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Ni Binding Site For Chain W'>AC1</scene>. Full crystallographic information is available from [http:// | 2C2L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=NI:'>NI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Ni+Binding+Site+For+Chain+W'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C2L OCA]. | ||
==Reference== | ==Reference== | ||
| Line 23: | Line 23: | ||
[[Category: ubiquitinylation]] | [[Category: ubiquitinylation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:30:39 2008'' | ||
Revision as of 11:30, 3 February 2008
|
CRYSTAL STRUCTURE OF THE CHIP U-BOX E3 UBIQUITIN LIGASE
OverviewOverview
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 StructureAbout 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.
ReferenceReference
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 Feb 3 10:30:39 2008