1p3q

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{{STRUCTURE_1p3q| PDB=1p3q | SCENE= }}
{{STRUCTURE_1p3q| PDB=1p3q | SCENE= }}
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'''Mechanism of Ubiquitin Recognition by the CUE Domain of VPS9'''
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===Mechanism of Ubiquitin Recognition by the CUE Domain of VPS9===
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==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.
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==About this Structure==
==About this Structure==
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[[Category: Post translational modification]]
[[Category: Post translational modification]]
[[Category: Trafficking]]
[[Category: Trafficking]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:38:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:07:00 2008''

Revision as of 02:07, 29 July 2008

Template:STRUCTURE 1p3q

Mechanism of Ubiquitin Recognition by the CUE Domain of VPS9

Template:ABSTRACT PUBMED 12787502

About this Structure

1P3Q is a Protein complex structure of sequences from Bos taurus and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

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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