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1otr
From Proteopedia
(New page: 200px<br /><applet load="1otr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1otr" /> '''Solution Structure of a CUE-Ubiquitin Comple...) |
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| - | [[Image:1otr.gif|left|200px]]<br /><applet load="1otr" size=" | + | [[Image:1otr.gif|left|200px]]<br /><applet load="1otr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1otr" /> | caption="1otr" /> | ||
'''Solution Structure of a CUE-Ubiquitin Complex'''<br /> | '''Solution Structure of a CUE-Ubiquitin Complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Monoubiquitination serves as a regulatory signal in a variety of cellular | + | 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== | ==About this Structure== | ||
| - | 1OTR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 1OTR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OTR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Daniels, C | + | [[Category: Daniels, C M.]] |
| - | [[Category: Kang, R | + | [[Category: Kang, R S.]] |
[[Category: Radhakrishnan, I.]] | [[Category: Radhakrishnan, I.]] | ||
| - | [[Category: Salerno, W | + | [[Category: Salerno, W J.]] |
[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:27 2008'' |
Revision as of 12:21, 21 February 2008
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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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