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6at5

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Current revision (06:54, 4 April 2018) (edit) (undo)
 
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<StructureSection load='6at5' size='340' side='right' caption='[[6at5]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='6at5' size='340' side='right' caption='[[6at5]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6at5]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AT5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AT5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6at5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AT5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AT5 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6at6|6at6]], [[6avf|6avf]], [[6avg|6avg]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6at6|6at6]], [[6avf|6avf]], [[6avg|6avg]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HLA-B, HLAB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), B2M, CDABP0092, HDCMA22P ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6at5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6at5 OCA], [http://pdbe.org/6at5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6at5 RCSB], [http://www.ebi.ac.uk/pdbsum/6at5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6at5 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6at5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6at5 OCA], [http://pdbe.org/6at5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6at5 RCSB], [http://www.ebi.ac.uk/pdbsum/6at5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6at5 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/1B07_HUMAN 1B07_HUMAN]] Involved in the presentation of foreign antigens to the immune system. [[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
[[http://www.uniprot.org/uniprot/1B07_HUMAN 1B07_HUMAN]] Involved in the presentation of foreign antigens to the immune system. [[http://www.uniprot.org/uniprot/B2MG_HUMAN B2MG_HUMAN]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human leukocyte antigen (HLA)-I molecules generally bind short peptides (8-10 amino acids), although extended HLA-I restricted peptides (&gt;10 amino acids) can be presented to T cells. However, the function of such extended HLA-I epitopes in tumour immunity, and how they would be recognised by T-cell receptors (TCR) remains unclear. Here we show that the structures of two distinct TCRs (TRAV4(+)TRAJ21(+)-TRBV28(+)TRBJ2-3(+) and TRAV4 (+) TRAJ8(+)-TRBV9(+)TRBJ2-1(+)), originating from a polyclonal T-cell repertoire, bind to HLA-B*07:02, presenting a 13-amino-acid-long tumour-associated peptide, NY-ESO-160-72. Comparison of the structures reveals that the two TCRs differentially binds NY-ESO-160-72-HLA-B*07:02 complex, and induces differing extent of conformational change of the NY-ESO-160-72 epitope. Accordingly, polyclonal TCR usage towards an extended HLA-I restricted tumour epitope translates to differing TCR recognition modes, whereby extensive flexibility at the TCR-pHLA-I interface engenders recognition.
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Divergent T-cell receptor recognition modes of a HLA-I restricted extended tumour-associated peptide.,Chan KF, Gully BS, Gras S, Beringer DX, Kjer-Nielsen L, Cebon J, McCluskey J, Chen W, Rossjohn J Nat Commun. 2018 Mar 12;9(1):1026. doi: 10.1038/s41467-018-03321-w. PMID:29531227<ref>PMID:29531227</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6at5" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Beta-2 microglobulin|Beta-2 microglobulin]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
[[Category: Gully, B S]]
[[Category: Gully, B S]]
[[Category: Rossjohn, J]]
[[Category: Rossjohn, J]]

Current revision

Crystal structure of HLA-B*07:02 in complex with an NY-ESO-1 peptide

6at5, resolution 1.50Å

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