3t6a: Difference between revisions

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==Structure of the C-terminal domain of BCAR3==
==Structure of the C-terminal domain of BCAR3==
<StructureSection load='3t6a' size='340' side='right' caption='[[3t6a]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3t6a' size='340' side='right'caption='[[3t6a]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3t6a]] 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=3T6A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T6A FirstGlance]. <br>
<table><tr><td colspan='2'>[[3t6a]] 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=3T6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T6A FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=POG:(20S)-2,5,8,11,14,17-HEXAMETHYL-3,6,9,12,15,18-HEXAOXAHENICOSANE-1,20-DIOL'>POG</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t6g|3t6g]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=POG:(20S)-2,5,8,11,14,17-HEXAMETHYL-3,6,9,12,15,18-HEXAOXAHENICOSANE-1,20-DIOL'>POG</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCAR3, NSP2, SH2D3B, UNQ271/PRO308 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3t6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t6a OCA], [https://pdbe.org/3t6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t6a RCSB], [https://www.ebi.ac.uk/pdbsum/3t6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t6a ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3t6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t6a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3t6a RCSB], [http://www.ebi.ac.uk/pdbsum/3t6a PDBsum]</span></td></tr>
</table>
<table>
== Function ==
<div style="background-color:#fffaf0;">
[https://www.uniprot.org/uniprot/BCAR3_HUMAN BCAR3_HUMAN] May act as an adapter protein and couple activated growth factor receptors to a signaling pathway that regulates the proliferation in breast cancer cells. When overexpressed, it confers anti-estrogen resistance in breast cancer cell lines. May also be regulated by cellular adhesion to extracellular matrix proteins.<ref>PMID:9582273</ref>  
== Publication Abstract from PubMed ==
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.
 
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>
 
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Mace, P D.]]
[[Category: Large Structures]]
[[Category: Riedl, S J.]]
[[Category: Mace PD]]
[[Category: Robinson, H.]]
[[Category: Riedl SJ]]
[[Category: Cdc25-homology domain]]
[[Category: Robinson H]]
[[Category: Gtpase exchange factor]]
[[Category: Signaling protein]]

Latest revision as of 10:04, 1 March 2024

Structure of the C-terminal domain of BCAR3

3t6a, resolution 2.40Å

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