1mn3: Difference between revisions

Revision as of 00:26, 3 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:1mn3.png

Template:STRUCTURE 1mn3

Cue domain of yeast Vps9pCue domain of yeast Vps9p

Template:ABSTRACT PUBMED 12787502

About this StructureAbout this Structure

1MN3 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Mechanism of ubiquitin recognition by the CUE domain of Vps9p., Prag G, Misra S, Jones EA, Ghirlando R, Davies BA, Horazdovsky BF, Hurley JH, Cell. 2003 May 30;113(5):609-20. PMID:12787502

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OCA

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-'''Cue domain of yeast Vps9p'''
+===Cue domain of yeast Vps9p===
-==Overview==
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-Coupling of ubiquitin conjugation to ER degradation (CUE) domains are approximately 50 amino acid monoubiquitin binding motifs found in proteins of trafficking and ubiquitination pathways. The 2.3 A structure of the Vps9p-CUE domain is a dimeric domain-swapped variant of the ubiquitin binding UBA domain. The 1.7 A structure of the CUE:ubiquitin complex shows that one CUE dimer binds one ubiquitin molecule. The bound CUE dimer is kinked relative to the unbound CUE dimer and wraps around ubiquitin. The CUE monomer contains two ubiquitin binding surfaces on opposite faces of the molecule that cannot bind simultaneously to a single ubiquitin molecule. Dimerization of the CUE domain allows both surfaces to contact a single ubiquitin molecule, providing a mechanism for high-affinity binding to monoubiquitin.
+The line below this paragraph, {{ABSTRACT_PUBMED_12787502}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Prag, G.]]
 [[Category: Ubiquitin]]
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