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| {{STRUCTURE_2e33| PDB=2e33 | SCENE= }} | | {{STRUCTURE_2e33| PDB=2e33 | SCENE= }} |
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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=== |
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| ==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 |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17389369 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17389369}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Scf]] | | [[Category: Scf]] |
| [[Category: Ubiquitin]] | | [[Category: Ubiquitin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:50:06 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:49:24 2008'' |
