View source for 9ytf


==TCR mimic antibody vAB-30 in complex with MAGE-A3 in HLA-A1==
<StructureSection load='9ytf' size='340' side='right'caption='[[9ytf]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ytf]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9YTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9YTF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6&#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=9ytf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ytf OCA], [https://pdbe.org/9ytf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ytf RCSB], [https://www.ebi.ac.uk/pdbsum/9ytf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ytf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1D3TZM3_HUMAN A0A1D3TZM3_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Class I major histocompatibility complexes (MHCs), expressed on the surface of all nucleated cells, present peptides derived from intracellular proteins for surveillance by T cells. The precise recognition of foreign or mutated peptide-MHC (pMHC) complexes by T cell receptors (TCRs) is central to immune defense against pathogens and tumors. Although patient-derived TCRs specific for cancer-associated antigens have been used to engineer tumor-targeting therapies, their reactivity toward self- or near-self antigens may be constrained by negative selection in the thymus. Here, we introduce a structure-based deep learning framework, ADAPT (Antigen-receptor Design Against Peptide-MHC Targets), for the design of TCRs and antibodies that bind to pMHC targets of interest. We evaluate the ADAPT pipeline by designing and characterizing TCRs and antibodies against a diverse panel of pMHCs. Cryogenic electron microscopy structures of two designed antibodies bound to their respective pMHC targets demonstrate atomic-level accuracy at the recognition interface, supporting the robustness of our structure-based approach. Computationally designed TCRs and antibodies targeting pMHC complexes could enable a broad range of therapeutic applications, from cancer immunotherapy to autoimmune disease treatment, and insights gained from TCR-pMHC design should advance predictive understanding of TCR specificity with implications for basic immunology and clinical diagnostics.

Targeting peptide-MHC complexes with designed T cell receptors and antibodies.,Motmaen A, Jude KM, Wang N, Minervina A, Feldman D, Lichtenstein MA, Ebenezer A, Correnti C, Thomas PG, Garcia KC, Baker D, Bradley P bioRxiv [Preprint]. 2025 Nov 20:2025.11.19.689381. doi: , 10.1101/2025.11.19.689381. PMID:41332722<ref>PMID:41332722</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9ytf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Jude KM]]
[[Category: Wang N]]