4l8s: Difference between revisions
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== | ==Crystal structure of a human Valpha7.2/Vbeta13.3 MAIT TCR in complex with bovine MR1== | ||
[[4l8s]] is a 3 chain structure with sequence from [ | <StructureSection load='4l8s' size='340' side='right'caption='[[4l8s]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4l8s]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L8S FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KFP:N~6~-[(2-AMINO-4-OXO-3,4-DIHYDROPTERIDIN-6-YL)METHYL]-D-LYSINE'>KFP</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=4l8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l8s OCA], [https://pdbe.org/4l8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l8s RCSB], [https://www.ebi.ac.uk/pdbsum/4l8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l8s ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6P4G7_HUMAN Q6P4G7_HUMAN] | |||
<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 4l8s" style="background-color:#fffaf0;"></div> | ||
[[ | |||
==See Also== | |||
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | |||
[[Category: | *[[T-cell receptor 3D structures|T-cell receptor 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Bos taurus]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Adams EJ]] | |||
[[Category: Lopez-Sagaseta J]] | |||
Latest revision as of 13:44, 14 December 2022
Crystal structure of a human Valpha7.2/Vbeta13.3 MAIT TCR in complex with bovine MR1Crystal structure of a human Valpha7.2/Vbeta13.3 MAIT TCR in complex with bovine MR1
Structural highlights
FunctionPublication 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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