6o4z: Difference between revisions
New page: '''Unreleased structure''' The entry 6o4z is ON HOLD Authors: Ying, G., Bitra, A., Zajonc, D.M. Description: Structure of HLA-A2:01 with peptide MM92 [[Category: Unreleased Structures]... |
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==Structure of HLA-A2:01 with peptide MM92== | |||
<StructureSection load='6o4z' size='340' side='right'caption='[[6o4z]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6o4z]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Schaalia_radingae Schaalia radingae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O4Z 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]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <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=6o4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o4z OCA], [https://pdbe.org/6o4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o4z RCSB], [https://www.ebi.ac.uk/pdbsum/6o4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o4z ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A140T913_HUMAN A0A140T913_HUMAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Targeting CD8(+) T cells to recurrent tumor-specific mutations can profoundly contribute to cancer treatment. Some of these mutations are potential tumor antigens although they can be displayed by non-spliced epitopes only in a few patients, because of the low affinity of the mutated non-spliced peptides for the predominant HLA class I alleles. Here, we describe a pipeline that uses the large sequence variety of proteasome-generated spliced peptides and identifies spliced epitope candidates, which carry the mutations and bind the predominant HLA-I alleles with high affinity. They could be used in adoptive T cell therapy and other anti-cancer immunotherapies for large cohorts of cancer patients. As a proof of principle, the application of this pipeline led to the identification of a KRAS G12V mutation-carrying spliced epitope candidate, which is produced by proteasomes, transported by TAPs and efficiently presented by the most prevalent HLA class I molecules, HLA-A(*)02:01 complexes. | |||
An in silico-in vitro Pipeline Identifying an HLA-A(*)02:01(+) KRAS G12V(+) Spliced Epitope Candidate for a Broad Tumor-Immune Response in Cancer Patients.,Mishto M, Mansurkhodzhaev A, Ying G, Bitra A, Cordfunke RA, Henze S, Paul D, Sidney J, Urlaub H, Neefjes J, Sette A, Zajonc DM, Liepe J Front Immunol. 2019 Nov 15;10:2572. doi: 10.3389/fimmu.2019.02572. eCollection , 2019. PMID:31803176<ref>PMID:31803176</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Bitra | <div class="pdbe-citations 6o4z" style="background-color:#fffaf0;"></div> | ||
[[Category: Ying | |||
[[Category: Zajonc | ==See Also== | ||
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | |||
*[[MHC 3D structures|MHC 3D structures]] | |||
*[[MHC I 3D structures|MHC I 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Schaalia radingae]] | |||
[[Category: Bitra A]] | |||
[[Category: Ying G]] | |||
[[Category: Zajonc DM]] | |||
Latest revision as of 12:08, 9 October 2024
Structure of HLA-A2:01 with peptide MM92Structure of HLA-A2:01 with peptide MM92
Structural highlights
FunctionPublication Abstract from PubMedTargeting CD8(+) T cells to recurrent tumor-specific mutations can profoundly contribute to cancer treatment. Some of these mutations are potential tumor antigens although they can be displayed by non-spliced epitopes only in a few patients, because of the low affinity of the mutated non-spliced peptides for the predominant HLA class I alleles. Here, we describe a pipeline that uses the large sequence variety of proteasome-generated spliced peptides and identifies spliced epitope candidates, which carry the mutations and bind the predominant HLA-I alleles with high affinity. They could be used in adoptive T cell therapy and other anti-cancer immunotherapies for large cohorts of cancer patients. As a proof of principle, the application of this pipeline led to the identification of a KRAS G12V mutation-carrying spliced epitope candidate, which is produced by proteasomes, transported by TAPs and efficiently presented by the most prevalent HLA class I molecules, HLA-A(*)02:01 complexes. An in silico-in vitro Pipeline Identifying an HLA-A(*)02:01(+) KRAS G12V(+) Spliced Epitope Candidate for a Broad Tumor-Immune Response in Cancer Patients.,Mishto M, Mansurkhodzhaev A, Ying G, Bitra A, Cordfunke RA, Henze S, Paul D, Sidney J, Urlaub H, Neefjes J, Sette A, Zajonc DM, Liepe J Front Immunol. 2019 Nov 15;10:2572. doi: 10.3389/fimmu.2019.02572. eCollection , 2019. PMID:31803176[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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