21ex: Difference between revisions

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New page: '''Unreleased structure''' The entry 21ex is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 21ex is ON HOLD
==Wild tipe p53WT-HLA-A2==
<StructureSection load='21ex' size='340' side='right'caption='[[21ex]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[21ex]] is a 3 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=21EX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=21EX FirstGlance]. <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]] 2.021&#8491;</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=21ex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=21ex OCA], [https://pdbe.org/21ex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=21ex RCSB], [https://www.ebi.ac.uk/pdbsum/21ex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=21ex ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8WLS4_HUMAN Q8WLS4_HUMAN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Adoptive cell therapy (ACT) with tumor-specific T cells can mediate durable cancer regression. The main target of tumor-specific T cells are neoantigens resulting from mutations in self-antigens over the course of malignant transformation. To understand T-cell recognition of cancer neoantigens at the atomic level, we studied a T-cell receptor (TCR 4414A) that recognizes a neoepitope arising from a driver mutation in the p53 oncogene (p53(Y220D)) presented by HLA-A2. Here, we report the structure of TCR 4414A bound to HLA-A2 and p53(Y220D), as well as structures of unbound wild-type and mutant p53-HLA-A2 ligands. The structures reveal that the Y220D mutation induces a conformational change in the p53(Y220D) neoepitope that is detected by TCR 4414A, thereby rendering a normally cryptic self-peptide visible to T cells. The TCR minimizes interactions with the N- and C-terminal portions of p53(Y220D), which are identical in mutant and wild-type peptides, and instead focuses on the Y220D driver mutation at the peptide center. In this way, TCR 4414A achieves highly specific recognition of mutant over wild-type p53, a critical parameter for avoiding off-target toxicities in ACT.


Authors:  
Structural basis for T-cell receptor recognition of p53(Y220D), a human cancer neoantigen.,Duan Z, Zhao J, Wu J, Zhang Y, Yuan P, Zeng Y, Jin H, Mariuzza RA, Wu D Acta Crystallogr D Struct Biol. 2026 Sep 1;82(Pt 9):1082-1092. doi: , 10.1107/S2059798326007564. Epub 2026 Aug 14. PMID:42599692<ref>PMID:42599692</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 21ex" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Duan ZH]]
[[Category: Wu DC]]