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3t6g

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==Structure of the complex between NSP3 (SHEP1) and p130Cas==
==Structure of the complex between NSP3 (SHEP1) and p130Cas==
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<StructureSection load='3t6g' size='340' side='right' caption='[[3t6g]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='3t6g' size='340' side='right'caption='[[3t6g]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3t6g]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T6G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T6G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3t6g]] is a 4 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=3T6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T6G 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=ACT:ACETATE+ION'>ACT</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t6a|3t6a]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SH2D3C, NSP3, UNQ272/PRO309/PRO34088 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), BCAR1, CAS, CASS1, CRKAS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3t6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t6g OCA], [https://pdbe.org/3t6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t6g RCSB], [https://www.ebi.ac.uk/pdbsum/3t6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t6g ProSAT]</span></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=3t6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t6g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t6g RCSB], [http://www.ebi.ac.uk/pdbsum/3t6g PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SH2D3_HUMAN SH2D3_HUMAN]] Eph receptor-binding protein which may be a positive regulator of TCR signaling. Binding to BCAR1 is required to induce membrane ruffling and promote EGF-dependent cell migration (By similarity). [[http://www.uniprot.org/uniprot/BCAR1_HUMAN BCAR1_HUMAN]] Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells.<ref>PMID:12832404</ref> <ref>PMID:17038317</ref>
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[https://www.uniprot.org/uniprot/SH2D3_HUMAN SH2D3_HUMAN] Eph receptor-binding protein which may be a positive regulator of TCR signaling. Binding to BCAR1 is required to induce membrane ruffling and promote EGF-dependent cell migration (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Members of the novel SH2-containing protein (NSP) and Crk-associated substrate (Cas) protein families form multidomain signaling platforms that mediate cell migration and invasion through a collection of distinct signaling motifs. Members of each family interact via their respective C-terminal domains, but the mechanism of this association has remained enigmatic. Here we present the crystal structures of the C-terminal domain from the NSP protein BCAR3 and the complex of NSP3 with p130Cas. BCAR3 adopts the Cdc25-homology fold of Ras GTPase exchange factors, but it has a 'closed' conformation incapable of enzymatic activity. The structure of the NSP3-p130Cas complex reveals that this closed conformation is instrumental for interaction of NSP proteins with a focal adhesion-targeting domain present in Cas proteins. This enzyme-to-adaptor conversion enables high-affinity, yet promiscuous, interactions between NSP and Cas proteins and represents an unprecedented mechanistic paradigm linking cellular signaling networks.
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NSP-Cas protein structures reveal a promiscuous interaction module in cell signaling.,Mace PD, Wallez Y, Dobaczewska MK, Lee JJ, Robinson H, Pasquale EB, Riedl SJ Nat Struct Mol Biol. 2011 Nov 13. doi: 10.1038/nsmb.2152. PMID:22081014<ref>PMID:22081014</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Mace, P D]]
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[[Category: Large Structures]]
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[[Category: Riedl, S J]]
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[[Category: Mace PD]]
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[[Category: Robinson, H]]
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[[Category: Riedl SJ]]
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[[Category: Cdc25-homology domain]]
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[[Category: Robinson H]]
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[[Category: Cell adhesion]]
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[[Category: Focal-adhesion targeting domain]]
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[[Category: Gtpase exchange factor]]
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[[Category: Signaling protein]]
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Current revision

Structure of the complex between NSP3 (SHEP1) and p130Cas

PDB ID 3t6g

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