2p64

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{{STRUCTURE_2p64| PDB=2p64 | SCENE= }}
{{STRUCTURE_2p64| PDB=2p64 | SCENE= }}
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'''D domain of b-TrCP'''
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===D domain of b-TrCP===
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==Overview==
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SCF ubiquitin ligases recruit substrates for degradation via F box protein adaptor subunits. WD40 repeat F box proteins, such as Cdc4 and beta-TrCP, contain a conserved dimerization motif called the D domain. Here, we report that the D domain protomers of yeast Cdc4 and human beta-TrCP form a superhelical homotypic dimer. Disruption of the D domain compromises the activity of yeast SCF(Cdc4) toward the CDK inhibitor Sic1 and other substrates. SCF(Cdc4) dimerization has little effect on the affinity for Sic1 but markedly stimulates ubiquitin conjugation. A model of the dimeric holo-SCF(Cdc4) complex based on small-angle X-ray scatter measurements reveals a suprafacial configuration, in which substrate-binding sites and E2 catalytic sites lie in the same plane with a separation of 64 A within and 102 A between each SCF monomer. This spatial variability may accommodate diverse acceptor lysine geometries in both substrates and the elongating ubiquitin chain and thereby increase catalytic efficiency.
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{{ABSTRACT_PUBMED_17574027}}
==About this Structure==
==About this Structure==
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[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Right handed super-helical bundle]]
[[Category: Right handed super-helical bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:17:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:41:13 2008''

Revision as of 03:41, 29 July 2008

Template:STRUCTURE 2p64

D domain of b-TrCP

Template:ABSTRACT PUBMED 17574027

About this Structure

2P64 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination., Tang X, Orlicky S, Lin Z, Willems A, Neculai D, Ceccarelli D, Mercurio F, Shilton BH, Sicheri F, Tyers M, Cell. 2007 Jun 15;129(6):1165-76. PMID:17574027

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