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[[Image:1otr.gif|left|200px]]
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{{STRUCTURE_1otr|  PDB=1otr  |  SCENE=  }}
'''Solution Structure of a CUE-Ubiquitin Complex'''


==Solution Structure of a CUE-Ubiquitin Complex==
<StructureSection load='1otr' size='340' side='right'caption='[[1otr]]' scene=''>
== Structural highlights ==
<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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CUE2_YEAST CUE2_YEAST]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ot/1otr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1otr" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[3D structures of ubiquitin|3D structures of ubiquitin]]
[[Category: Protein complex]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Daniels, C M.]]
[[Category: Daniels CM]]
[[Category: Kang, R S.]]
[[Category: Kang RS]]
[[Category: Radhakrishnan, I.]]
[[Category: Radhakrishnan I]]
[[Category: Salerno, W J.]]
[[Category: Salerno WJ]]
[[Category: Protein-protein complex]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:16:25 2008''

Latest revision as of 08:57, 22 May 2024

Solution Structure of a CUE-Ubiquitin Complex

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