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4cc7

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<StructureSection load='4cc7' size='340' side='right'caption='[[4cc7]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
<StructureSection load='4cc7' size='340' side='right'caption='[[4cc7]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4cc7]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CC7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CC7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4cc7]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CC7 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cc7 OCA], [http://pdbe.org/4cc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cc7 RCSB], [http://www.ebi.ac.uk/pdbsum/4cc7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cc7 ProSAT]</span></td></tr>
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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=4cc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cc7 OCA], [https://pdbe.org/4cc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cc7 RCSB], [https://www.ebi.ac.uk/pdbsum/4cc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cc7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DNMBP_HUMAN DNMBP_HUMAN]] Scaffold protein that links dynamin with actin-regulating proteins. May play a role in membrane trafficking between the cell surface and the Golgi (By similarity). [[http://www.uniprot.org/uniprot/WASL_HUMAN WASL_HUMAN]] Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression.<ref>PMID:19366662</ref>
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[[https://www.uniprot.org/uniprot/DNMBP_HUMAN DNMBP_HUMAN]] Scaffold protein that links dynamin with actin-regulating proteins. May play a role in membrane trafficking between the cell surface and the Golgi (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The human pathogen Listeria monocytogenes is able to directly spread to neighboring cells of host tissues, a process recently linked to the virulence factor InlC. InlC targets the sixth SH3 domain (SH3-6) of human Tuba, disrupting its physiological interaction with the cytoskeletal protein N-WASP. The resulting loss of cortical actin tension may slacken the junctional membrane, allowing protrusion formation by motile Listeria. Complexes of Tuba SH3-6 with physiological partners N-WASP and Mena reveal equivalent binding modes but distinct affinities. The interaction surface of the infection complex InlC/Tuba SH3-6 is centered on phenylalanine 146 of InlC stacking upon asparagine 1569 of Tuba. Replacing Phe146 by alanine largely abrogates molecular affinity and in vivo mimics deletion of inlC. Collectively, our findings indicate that InlC hijacks Tuba through its LRR domain, blocking the peptide binding groove to prevent recruitment of its physiological partners.
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Structural Details of Human Tuba Recruitment by InlC of Listeria monocytogenes Elucidate Bacterial Cell-Cell Spreading.,Polle L, Rigano LA, Julian R, Ireton K, Schubert WD Structure. 2013 Dec 10. pii: S0969-2126(13)00429-2. doi:, 10.1016/j.str.2013.10.017. PMID:24332715<ref>PMID:24332715</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 4cc7" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Tuba 3D structures|Tuba 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ireton, K]]
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[[Category: Ireton K]]
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[[Category: Julian, R]]
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[[Category: Julian R]]
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[[Category: Polle, L]]
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[[Category: Polle L]]
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[[Category: Rigano, L]]
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[[Category: Rigano L]]
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[[Category: Schubert, W D]]
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[[Category: Schubert W-D]]
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[[Category: Actin cytoskeleton]]
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[[Category: Cell-cell contact]]
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[[Category: Cortical tension]]
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[[Category: Proline-rich peptide]]
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[[Category: Src homology 3]]
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[[Category: Structural protein]]
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Revision as of 17:38, 7 September 2022

Crystal structure of the sixth or C-terminal SH3 domain of human Tuba in complex with proline-rich peptides of N-WASP. Space group P41

PDB ID 4cc7

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