2jt4
From Proteopedia
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| - | [[Image:2jt4.png|left|200px]] | ||
| - | + | ==Solution Structure of the Sla1 SH3-3-Ubiquitin Complex== | |
| + | <StructureSection load='2jt4' size='340' side='right'caption='[[2jt4]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2jt4]] 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=2JT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JT4 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=2jt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jt4 OCA], [https://pdbe.org/2jt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jt4 RCSB], [https://www.ebi.ac.uk/pdbsum/2jt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jt4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SLA1_YEAST SLA1_YEAST] Component of the PAN1 actin cytoskeleton-regulatory complex required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton. Mediates uptake of external molecules and vacuolar degradation of plasma membrane proteins. Plays a role in the proper organization of the cell membrane-associated actin cytoskeleton and promotes its destabilization.<ref>PMID:8335689</ref> <ref>PMID:8756649</ref> <ref>PMID:9008707</ref> <ref>PMID:9128251</ref> <ref>PMID:10198057</ref> <ref>PMID:10594004</ref> <ref>PMID:11940605</ref> <ref>PMID:11950888</ref> <ref>PMID:12388763</ref> <ref>PMID:12237851</ref> <ref>PMID:12814545</ref> <ref>PMID:12734398</ref> <ref>PMID:14761940</ref> <ref>PMID:15525671</ref> <ref>PMID:17286805</ref> | ||
| + | == 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/jt/2jt4_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=2jt4 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The SH3 domain is a protein-protein interaction module commonly found in intracellular signaling and adaptor proteins. The SH3 domains of multiple endocytic proteins have been recently implicated in binding ubiquitin, which serves as a signal for diverse cellular processes including gene regulation, endosomal sorting, and protein destruction. Here we describe the solution NMR structure of ubiquitin in complex with an SH3 domain belonging to the yeast endocytic protein Sla1. The ubiquitin binding surface of the Sla1 SH3 domain overlaps substantially with the canonical binding surface for proline-rich ligands. Like many other ubiquitin-binding motifs, the SH3 domain engages the Ile44 hydrophobic patch of ubiquitin. A phenylalanine residue located at the heart of the ubiquitin-binding surface of the SH3 domain serves as a key specificity determinant. The structure of the SH3-ubiquitin complex explains how a subset of SH3 domains has acquired this non-traditional function. | ||
| - | + | Structural basis for ubiquitin recognition by SH3 domains.,He Y, Hicke L, Radhakrishnan I J Mol Biol. 2007 Oct 12;373(1):190-6. Epub 2007 Aug 17. PMID:17765920<ref>PMID:17765920</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2jt4" style="background-color:#fffaf0;"></div> | |
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==See Also== | ==See Also== | ||
| - | *[[ | + | *[[3D structures of ubiquitin|3D structures of ubiquitin]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: He | + | [[Category: He Y]] |
| - | [[Category: Radhakrishnan | + | [[Category: Radhakrishnan I]] |
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Current revision
Solution Structure of the Sla1 SH3-3-Ubiquitin Complex
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