2e32: Difference between revisions

Revision as of 14:03, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2e32.png

Template:STRUCTURE 2e32

Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligaseStructural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligase

Template:ABSTRACT PUBMED 17389369

About this StructureAbout this Structure

2E32 is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the selection of glycosylated substrates by SCF(Fbs1) ubiquitin ligase., Mizushima T, Yoshida Y, Kumanomidou T, Hasegawa Y, Suzuki A, Yamane T, Tanaka K, Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5777-81. Epub 2007 Mar 26. PMID:17389369

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligase'''
+===Structural basis for selection of glycosylated substrate by SCFFbs1 ubiquitin ligase===
-==Overview==
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-The ubiquitin ligase complex SCF(Fbs1), which contributes to the ubiquitination of glycoproteins, is involved in the endoplasmic reticulum-associated degradation pathway. In SCF ubiquitin ligases, a diverse array of F-box proteins confers substrate specificity. Fbs1/Fbx2, a member of the F-box protein family, recognizes high-mannose oligosaccharides. To elucidate the structural basis of SCF(Fbs1) function, we determined the crystal structures of the Skp1-Fbs1 complex and the sugar-binding domain (SBD) of the Fbs1-glycoprotein complex. The mechanistic model indicated by the structures appears to be well conserved among the SCF ubiquitin ligases. The structure of the SBD-glycoprotein complex indicates that the SBD primarily recognizes Man(3)GlcNAc(2), thereby explaining the broad activity of the enzyme against various glycoproteins. Comparison of two crystal structures of the Skp1-Fbs1 complex revealed the relative motion of a linker segment between the F-box and the SBD domains, which might underlie the ability of the complex to recognize different acceptor lysine residues for ubiquitination.
+The line below this paragraph, {{ABSTRACT_PUBMED_17389369}}, adds the Publication Abstract to the page
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 [[Category: Ubiquitin]]
 [[Category: Ubiquitin ligase]]
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