1otr
From Proteopedia
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[[Image:1otr.gif|left|200px]] | [[Image:1otr.gif|left|200px]] | ||
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'''Solution Structure of a CUE-Ubiquitin Complex''' | '''Solution Structure of a CUE-Ubiquitin Complex''' | ||
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[[Category: Radhakrishnan, I.]] | [[Category: Radhakrishnan, I.]] | ||
[[Category: Salerno, W J.]] | [[Category: Salerno, W J.]] | ||
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Revision as of 01:16, 3 May 2008
Solution Structure of a CUE-Ubiquitin Complex
Overview
Monoubiquitination serves as a regulatory signal in a variety of cellular processes. Monoubiquitin signals are transmitted by binding to a small but rapidly expanding class of ubiquitin binding motifs. Several of these motifs, including the CUE domain, also promote intramolecular monoubiquitination. The solution structure of a CUE domain of the yeast Cue2 protein in complex with ubiquitin reveals intermolecular interactions involving conserved hydrophobic surfaces, including the Leu8-Ile44-Val70 patch on ubiquitin. The contact surface extends beyond this patch and encompasses Lys48, a site of polyubiquitin chain formation. This suggests an occlusion mechanism for inhibiting polyubiquitin chain formation during monoubiquitin signaling. The CUE domain shares a similar overall architecture with the UBA domain, which also contains a conserved hydrophobic patch. Comparative modeling suggests that the UBA domain interacts analogously with ubiquitin. The structure of the CUE-ubiquitin complex may thus serve as a paradigm for ubiquitin recognition and signaling by ubiquitin binding proteins.
About this Structure
1OTR is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Solution structure of a CUE-ubiquitin complex reveals a conserved mode of ubiquitin binding., Kang RS, Daniels CM, Francis SA, Shih SC, Salerno WJ, Hicke L, Radhakrishnan I, Cell. 2003 May 30;113(5):621-30. PMID:12787503 Page seeded by OCA on Sat May 3 04:16:25 2008
