2mcn: Difference between revisions
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The | ==Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications== | ||
<StructureSection load='2mcn' size='340' side='right'caption='[[2mcn]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2mcn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MCN 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=2mcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mcn OCA], [https://pdbe.org/2mcn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mcn RCSB], [https://www.ebi.ac.uk/pdbsum/2mcn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mcn ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CD2AP_MOUSE CD2AP_MOUSE] Required for cytokinesis (By similarity). Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton. May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell. May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus.<ref>PMID:10514378</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
SH3 domains constitute a new type of ubiquitin-binding domains. We previously showed that the third SH3 domain (SH3-C) of CD2AP binds ubiquitin in an alternative orientation. We have determined the structure of the complex between first CD2AP SH3 domain and ubiquitin and performed a structural and mutational analysis to decipher the determinants of the SH3-C binding mode to ubiquitin. We found that the Phe-to-Tyr mutation in CD2AP and in the homologous CIN85 SH3-C domain does not abrogate ubiquitin binding, in contrast to previous hypothesis and our findings for the first two CD2AP SH3 domains. The similar alternative binding mode of the SH3-C domains of these related adaptor proteins is characterised by a higher affinity to C-terminal extended ubiquitin molecules. We conclude that CD2AP/CIN85 SH3-C domain interaction with ubiquitin constitutes a new ubiquitin-binding mode involved in a different cellular function and thus changes the previously established mechanism of EGF-dependent CD2AP/CIN85 mono-ubiquitination. | |||
Distinct Ubiquitin Binding Modes Exhibited by SH3 Domains: Molecular Determinants and Functional Implications.,Ortega Roldan JL, Casares S, Ringkjobing Jensen M, Cardenes N, Bravo J, Blackledge M, Azuaga AI, van Nuland NA PLoS One. 2013 Sep 11;8(9):e73018. doi: 10.1371/journal.pone.0073018. PMID:24039852<ref>PMID:24039852</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2mcn" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[CD2-associated protein 3D structures|CD2-associated protein 3D structures]] | |||
*[[3D structures of ubiquitin|3D structures of ubiquitin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Azuaga A]] | |||
[[Category: Blackledge M]] | |||
[[Category: Ortega-Roldan J]] | |||
[[Category: Salmon L]] | |||
[[Category: Van Nuland N]] | |||
Latest revision as of 06:04, 15 May 2024
Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications
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