1otr: Difference between revisions
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[[Image:1otr.gif|left|200px]]< | [[Image:1otr.gif|left|200px]] | ||
'''Solution Structure of a CUE-Ubiquitin Complex''' | {{Structure | ||
|PDB= 1otr |SIZE=350|CAPTION= <scene name='initialview01'>1otr</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= CUE2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), UBI1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |||
}} | |||
'''Solution Structure of a CUE-Ubiquitin Complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1OTR is a [ | 1OTR is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12787503 12787503] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:15:28 2008'' | ||
Revision as of 11:15, 20 March 2008
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| Gene: | CUE2 (Saccharomyces cerevisiae), UBI1 (Saccharomyces cerevisiae) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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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