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1otr

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[[Image:1otr.gif|left|200px]]
 
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{{Structure
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==Solution Structure of a CUE-Ubiquitin Complex==
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|PDB= 1otr |SIZE=350|CAPTION= <scene name='initialview01'>1otr</scene>
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<StructureSection load='1otr' size='340' side='right'caption='[[1otr]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1otr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OTR FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|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])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1otr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1otr OCA], [https://pdbe.org/1otr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1otr RCSB], [https://www.ebi.ac.uk/pdbsum/1otr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1otr ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1otr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1otr OCA], [http://www.ebi.ac.uk/pdbsum/1otr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1otr RCSB]</span>
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[https://www.uniprot.org/uniprot/CUE2_YEAST CUE2_YEAST]
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ot/1otr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1otr ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Solution Structure of a CUE-Ubiquitin Complex'''
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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<ref>PMID:12787503</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1otr" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[3D structures of ubiquitin|3D structures of ubiquitin]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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]
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[[Category: Protein complex]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Daniels, C M.]]
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[[Category: Daniels CM]]
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[[Category: Kang, R S.]]
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[[Category: Kang RS]]
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[[Category: Radhakrishnan, I.]]
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[[Category: Radhakrishnan I]]
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[[Category: Salerno, W J.]]
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[[Category: Salerno WJ]]
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[[Category: protein-protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:50:12 2008''
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Current revision

Solution Structure of a CUE-Ubiquitin Complex

PDB ID 1otr

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