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[[ | ==Structure of mouse Va14Vb8.2NKT TCR-mouse CD1d-a-C-Galactosylceramide complex== | ||
<StructureSection load='3tn0' size='340' side='right' caption='[[3tn0]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3tn0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TN0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TN0 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=QUX:N-[(3S,4S,5R)-4,5-DIHYDROXY-1-[(2R,3R,4R,5R,6R)-3,4,5-TRIHYDROXY-6-(HYDROXYMETHYL)OXAN-2-YL]NONADECAN-3-YL]HEXACOSANAMIDE'>QUX</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qux|3qux]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cd1d1, Cd1.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), B2m, RP23-34E24.5-001, mCG_11606 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3tn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tn0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tn0 RCSB], [http://www.ebi.ac.uk/pdbsum/3tn0 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
NKT cells respond to a variety of CD1d-restricted glycolipid Ags that are structurally related to the prototypic Ag alpha-galactosylceramide (alpha-GalCer). A modified analog of alpha-GalCer with a carbon-based glycosidic linkage (alpha-C-GalCer) has generated great interest because of its apparent ability to promote prolonged, Th1-biased immune responses. In this study, we report the activation of spleen NKT cells to alpha-C-GalCer, and related C-glycoside ligands, is weaker than that of alpha-GalCer. Furthermore, the Vbeta8.2 and Vbeta7 NKT TCR affinity for CD1d-alpha-C-GalCer, and some related analogs, is approximately 10-fold lower than that for the NKT TCR-CD1d-alpha-GalCer interaction. Nevertheless, the crystal structure of the Vbeta8.2 NKT TCR-CD1d-alpha-C-GalCer complex is similar to that of the corresponding NKT TCR-CD1d-alpha-GalCer complex, although subtle differences at the interface provide a basis for understanding the lower affinity of the NKT TCR-CD1d-alpha-C-GalCer interaction. Our findings support the concept that for CD1d-restricted NKT cells, altered glycolipid ligands can promote markedly different responses while adopting similar TCR-docking topologies. | |||
NKT TCR recognition of CD1d-alpha-C-galactosylceramide.,Patel O, Cameron G, Pellicci DG, Liu Z, Byun HS, Beddoe T, McCluskey J, Franck RW, Castano AR, Harrak Y, Llebaria A, Bittman R, Porcelli SA, Godfrey DI, Rossjohn J J Immunol. 2011 Nov 1;187(9):4705-13. Epub 2011 Sep 30. PMID:21964029<ref>PMID:21964029</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Beta-2 microglobulin|Beta-2 microglobulin]] | *[[Beta-2 microglobulin|Beta-2 microglobulin]] | ||
*[[CD1|CD1]] | |||
== | == References == | ||
< | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Patel, O | [[Category: Patel, O]] | ||
[[Category: Rossjohn, J | [[Category: Rossjohn, J]] | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
[[Category: Mouse cd1d]] | [[Category: Mouse cd1d]] | ||
[[Category: Mouse nkt]] | [[Category: Mouse nkt]] | ||
Revision as of 19:27, 9 December 2014
Structure of mouse Va14Vb8.2NKT TCR-mouse CD1d-a-C-Galactosylceramide complexStructure of mouse Va14Vb8.2NKT TCR-mouse CD1d-a-C-Galactosylceramide complex
Structural highlights
Publication Abstract from PubMedNKT cells respond to a variety of CD1d-restricted glycolipid Ags that are structurally related to the prototypic Ag alpha-galactosylceramide (alpha-GalCer). A modified analog of alpha-GalCer with a carbon-based glycosidic linkage (alpha-C-GalCer) has generated great interest because of its apparent ability to promote prolonged, Th1-biased immune responses. In this study, we report the activation of spleen NKT cells to alpha-C-GalCer, and related C-glycoside ligands, is weaker than that of alpha-GalCer. Furthermore, the Vbeta8.2 and Vbeta7 NKT TCR affinity for CD1d-alpha-C-GalCer, and some related analogs, is approximately 10-fold lower than that for the NKT TCR-CD1d-alpha-GalCer interaction. Nevertheless, the crystal structure of the Vbeta8.2 NKT TCR-CD1d-alpha-C-GalCer complex is similar to that of the corresponding NKT TCR-CD1d-alpha-GalCer complex, although subtle differences at the interface provide a basis for understanding the lower affinity of the NKT TCR-CD1d-alpha-C-GalCer interaction. Our findings support the concept that for CD1d-restricted NKT cells, altered glycolipid ligands can promote markedly different responses while adopting similar TCR-docking topologies. NKT TCR recognition of CD1d-alpha-C-galactosylceramide.,Patel O, Cameron G, Pellicci DG, Liu Z, Byun HS, Beddoe T, McCluskey J, Franck RW, Castano AR, Harrak Y, Llebaria A, Bittman R, Porcelli SA, Godfrey DI, Rossjohn J J Immunol. 2011 Nov 1;187(9):4705-13. Epub 2011 Sep 30. PMID:21964029[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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