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== | ==Crystal structure of a human MAIT TCR in complex with a bacterial antigen bound to humanized bovine MR1== | ||
[[4lcc]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LCC OCA]. | <StructureSection load='4lcc' size='340' side='right' caption='[[4lcc]], [[Resolution|resolution]] 3.26Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4lcc]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LCC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LCC FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1XL:1-DEOXY-1-[6-(HYDROXYMETHYL)-2,4-DIOXO-3,4-DIHYDROPTERIDIN-8(2H)-YL]-D-ARABINITOL'>1XL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4iiq|4iiq]], [[4l8s|4l8s]], [[4l9l|4l9l]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MR1, Bt.63045 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</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=4lcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lcc OCA], [http://pdbe.org/4lcc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lcc RCSB], [http://www.ebi.ac.uk/pdbsum/4lcc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lcc ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
MR1-restricted mucosal-associated invariant T (MAIT) cells represent a subpopulation of alphabeta T cells with innate-like properties and limited TCR diversity. MAIT cells are of interest because of their reactivity against bacterial and yeast species, suggesting that they play a role in defense against pathogenic microbes. Despite the advances in understanding MAIT cell biology, the molecular and structural basis behind their ability to detect MR1-Ag complexes is unclear. In this study, we present our structural and biochemical characterization of MAIT TCR engagement of MR1 presenting an Escherichia coli-derived stimulatory ligand, rRL-6-CH2OH, previously found in Salmonella typhimurium. We show a clear enhancement of MAIT TCR binding to MR1 due to the presentation of this ligand. Our structure of a MAIT TCR/MR1/rRL-6-CH2OH complex shows an evolutionarily conserved binding orientation, with a clear role for both the CDR3alpha and CDR3beta loops in recognizing the rRL-6-CH2OH stimulatory ligand. We also present two additional xenoreactive MAIT TCR/MR1 complexes that recapitulate the docking orientation documented previously, despite having variation in the CDR2beta and CDR3beta loop sequences. Our data support a model by which MAIT TCRs engage MR1 in a conserved fashion, with their binding affinities modulated by the nature of the MR1-presented Ag or diversity introduced by alternate Vbeta usage or CDR3beta sequences. | |||
MAIT Recognition of a Stimulatory Bacterial Antigen Bound to MR1.,Lopez-Sagaseta J, Dulberger CL, McFedries A, Cushman M, Saghatelian A, Adams EJ J Immunol. 2013 Nov 15;191(10):5268-77. doi: 10.4049/jimmunol.1301958. Epub 2013 , Oct 9. PMID:24108697<ref>PMID:24108697</ref> | |||
<ref | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4lcc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-2 microglobulin|Beta-2 microglobulin]] | |||
*[[T-cell receptor|T-cell receptor]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bovin]] | [[Category: Bovin]] | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Adams, E J]] | [[Category: Adams, E J]] | ||
[[Category: Lopez-Sagaseta, J | [[Category: Lopez-Sagaseta, J]] | ||
[[Category: Antigen presentation]] | [[Category: Antigen presentation]] | ||
[[Category: Antigen recognition]] | [[Category: Antigen recognition]] | ||
Revision as of 23:24, 11 August 2016
Crystal structure of a human MAIT TCR in complex with a bacterial antigen bound to humanized bovine MR1Crystal structure of a human MAIT TCR in complex with a bacterial antigen bound to humanized bovine MR1
Structural highlights
Publication Abstract from PubMedMR1-restricted mucosal-associated invariant T (MAIT) cells represent a subpopulation of alphabeta T cells with innate-like properties and limited TCR diversity. MAIT cells are of interest because of their reactivity against bacterial and yeast species, suggesting that they play a role in defense against pathogenic microbes. Despite the advances in understanding MAIT cell biology, the molecular and structural basis behind their ability to detect MR1-Ag complexes is unclear. In this study, we present our structural and biochemical characterization of MAIT TCR engagement of MR1 presenting an Escherichia coli-derived stimulatory ligand, rRL-6-CH2OH, previously found in Salmonella typhimurium. We show a clear enhancement of MAIT TCR binding to MR1 due to the presentation of this ligand. Our structure of a MAIT TCR/MR1/rRL-6-CH2OH complex shows an evolutionarily conserved binding orientation, with a clear role for both the CDR3alpha and CDR3beta loops in recognizing the rRL-6-CH2OH stimulatory ligand. We also present two additional xenoreactive MAIT TCR/MR1 complexes that recapitulate the docking orientation documented previously, despite having variation in the CDR2beta and CDR3beta loop sequences. Our data support a model by which MAIT TCRs engage MR1 in a conserved fashion, with their binding affinities modulated by the nature of the MR1-presented Ag or diversity introduced by alternate Vbeta usage or CDR3beta sequences. MAIT Recognition of a Stimulatory Bacterial Antigen Bound to MR1.,Lopez-Sagaseta J, Dulberger CL, McFedries A, Cushman M, Saghatelian A, Adams EJ J Immunol. 2013 Nov 15;191(10):5268-77. doi: 10.4049/jimmunol.1301958. Epub 2013 , Oct 9. PMID:24108697[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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