6vth
From Proteopedia
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<StructureSection load='6vth' size='340' side='right'caption='[[6vth]], [[Resolution|resolution]] 2.36Å' scene=''> | <StructureSection load='6vth' size='340' side='right'caption='[[6vth]], [[Resolution|resolution]] 2.36Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VTH FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.36Å</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6vth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vth OCA], [https://pdbe.org/6vth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vth RCSB], [https://www.ebi.ac.uk/pdbsum/6vth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vth ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Adoptive cell therapy (ACT) with tumor-specific T cells can mediate cancer regression. The main target of tumor-specific T cells are neoantigens arising from mutations in self-proteins. Although the majority of cancer neoantigens are unique to each patient, and therefore not broadly useful for ACT, some are shared. We studied oligoclonal T-cell receptors (TCRs) that recognize a shared neoepitope arising from a driver mutation in the p53 oncogene (p53R175H) presented by HLA-A2. Here we report structures of wild-type and mutant p53-HLA-A2 ligands, as well as structures of three tumor-specific TCRs bound to p53R175H-HLA-A2. These structures reveal how a driver mutation in p53 rendered a self-peptide visible to T cells. The TCRs employ structurally distinct strategies that are highly focused on the mutation to discriminate between mutant and wild-type p53. The TCR-p53R175H-HLA-A2 complexes provide a framework for designing TCRs to improve potency for ACT without sacrificing specificity. | ||
- | + | ==See Also== | |
- | + | *[[T-cell receptor 3D structures|T-cell receptor 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Gallagher | + | [[Category: Gallagher DT]] |
- | [[Category: Gowthaman | + | [[Category: Gowthaman R]] |
- | [[Category: Mariuzza | + | [[Category: Mariuzza RA]] |
- | [[Category: Pierce | + | [[Category: Pierce BG]] |
- | [[Category: Wu | + | [[Category: Wu D]] |
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Current revision
p53-specific T cell receptor
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