6at6: Difference between revisions
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<StructureSection load='6at6' size='340' side='right' caption='[[6at6]], [[Resolution|resolution]] 1.42Å' scene=''> | <StructureSection load='6at6' size='340' side='right' caption='[[6at6]], [[Resolution|resolution]] 1.42Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6at6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AT6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6at6]] is a 2 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=6AT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AT6 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6at5|6at5]], [[6avf|6avf]], [[6avg|6avg]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6at5|6at5]], [[6avf|6avf]], [[6avg|6avg]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B2M, HDCMA22P ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), TRAV4 ([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=6at6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6at6 OCA], [http://pdbe.org/6at6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6at6 RCSB], [http://www.ebi.ac.uk/pdbsum/6at6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6at6 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=6at6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6at6 OCA], [http://pdbe.org/6at6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6at6 RCSB], [http://www.ebi.ac.uk/pdbsum/6at6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6at6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Human leukocyte antigen (HLA)-I molecules generally bind short peptides (8-10 amino acids), although extended HLA-I restricted peptides (>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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6at6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Gully, B S]] | [[Category: Gully, B S]] | ||
[[Category: Rossjohn, J]] | [[Category: Rossjohn, J]] | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
[[Category: Immunogolbulin]] | [[Category: Immunogolbulin]] | ||
Revision as of 09:54, 4 April 2018
Crystal structure of the KFJ5 TCRCrystal structure of the KFJ5 TCR
Structural highlights
Publication Abstract from PubMedHuman leukocyte antigen (HLA)-I molecules generally bind short peptides (8-10 amino acids), although extended HLA-I restricted peptides (>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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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