4y16: Difference between revisions
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==Crystal structure of the mCD1d/NC-aGC/iNKTCR ternary complex== | ==Crystal structure of the mCD1d/NC-aGC/iNKTCR ternary complex== | ||
<StructureSection load='4y16' size='340' side='right' caption='[[4y16]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='4y16' size='340' side='right'caption='[[4y16]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4y16]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y16 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4y16]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y16 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y16 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=48G:N-[(2S,3S,4R)-3,4-DIHYDROXY-1-{[6-O-(NAPHTHALEN-1-YLCARBAMOYL)-ALPHA-D-GALACTOPYRANOSYL]OXY}OCTADECAN-2-YL]HEXACOSANAMIDE'>48G</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=48G:N-[(2S,3S,4R)-3,4-DIHYDROXY-1-{[6-O-(NAPHTHALEN-1-YLCARBAMOYL)-ALPHA-D-GALACTOPYRANOSYL]OXY}OCTADECAN-2-YL]HEXACOSANAMIDE'>48G</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4y16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y16 OCA], [https://pdbe.org/4y16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y16 RCSB], [https://www.ebi.ac.uk/pdbsum/4y16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y16 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CD1D1_MOUSE CD1D1_MOUSE] Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells.<ref>PMID:11754812</ref> <ref>PMID:16314439</ref> <ref>PMID:16007091</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Beta-2 microglobulin|Beta-2 microglobulin]] | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | ||
*[[T-cell receptor|T-cell receptor]] | *[[CD1|CD1]] | ||
*[[T-cell receptor 3D structures|T-cell receptor 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: | [[Category: Nemcovic M]] | ||
[[Category: | [[Category: Zajonc DM]] | ||
Latest revision as of 10:53, 27 September 2023
Crystal structure of the mCD1d/NC-aGC/iNKTCR ternary complexCrystal structure of the mCD1d/NC-aGC/iNKTCR ternary complex
Structural highlights
FunctionCD1D1_MOUSE Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells.[1] [2] [3] Publication Abstract from PubMedThe ability of different glycosphingolipids (GSLs) to activate Type I Natural Killer T cells (iNKT cells) has been known for two decades. The possible therapeutic use of these GSLs has been studied in many ways, however studies in which the efficacy of promising GSLs is compared under identical conditions are missing. Here we compare five unique GSLs structurally derived from alpha-galactosylceramide (alphaGalCer). We employed biophysical and biological assays, as well as X-ray crystallography to study the impact of the chemical modifications of the antigen on Type I NKT cell activation. While all glycolipids are bound by the TCR of Type I NKT cells in real-time binding assays with high affinity, only a few activate Type I NKT cells in in vivo or in vitro experiments. The differences in biological responses are likely a result of different pharmacokinetic properties of each lipid, which carry modifications at different parts of the molecule. Our results indicate a need to perform a variety of assays to ascertain the therapeutic potential of Type I NKT cell GSL activators. Lipid and carbohydrate modifications of alpha-galactosylceramide differently influence mouse and human type I natural killer T cell activation.,Birkholz A, Nemcovic M, Yu ED, Girardi E, Wang J, Khurana A, Pauwels N, Farber E, Chitale S, Franck RW, Tsuji M, Howell A, Van Calenbergh S, Kronenberg M, Zajonc DM J Biol Chem. 2015 May 27. pii: jbc.M115.654814. PMID:26018083[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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