1otr
From Proteopedia
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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
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