6xng
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==MHC-like protein complex structure== |
| - | <StructureSection load='6xng' size='340' side='right'caption='[[6xng]]' scene=''> | + | <StructureSection load='6xng' size='340' side='right'caption='[[6xng]], [[Resolution|resolution]] 2.79Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6xng]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XNG FirstGlance]. <br> |
| - | </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=6xng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xng OCA], [https://pdbe.org/6xng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xng RCSB], [https://www.ebi.ac.uk/pdbsum/6xng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xng ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.79Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=V8P:(3R)-N-[(2S,3R)-1-(alpha-D-galactopyranosyloxy)-3-hydroxyheptadecan-2-yl]-3-hydroxyheptadecanamide'>V8P</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=6xng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xng OCA], [https://pdbe.org/6xng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xng RCSB], [https://www.ebi.ac.uk/pdbsum/6xng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xng ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == 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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Small molecules derived from symbiotic microbiota critically contribute to intestinal immune maturation and regulation(1). However, little is known about the molecular mechanisms that control immune development in the host-microbiota environment. Here, using a targeted lipidomic analysis and synthetic approach, we carried out a multifaceted investigation of immunomodulatory alpha-galactosylceramides from the human symbiont Bacteroides fragilis (BfaGCs). The characteristic terminal branching of BfaGCs is the result of incorporation of branched-chain amino acids taken up in the host gut by B. fragilis. A B. fragilis knockout strain that cannot metabolize branched-chain amino acids showed reduced branching in BfaGCs, and mice monocolonized with this mutant strain had impaired colonic natural killer T (NKT) cell regulation, implying structure-specific immunomodulatory activity. The sphinganine chain branching of BfaGCs is a critical determinant of NKT cell activation, which induces specific immunomodulatory gene expression signatures and effector functions. Co-crystal structure and affinity analyses of CD1d-BfaGC-NKT cell receptor complexes confirmed the interaction of BfaGCs as CD1d-restricted ligands. We present a structural and molecular-level paradigm of immunomodulatory control by interactions of endobiotic metabolites with diet, microbiota and the immune system. | ||
| + | |||
| + | Host immunomodulatory lipids created by symbionts from dietary amino acids.,Oh SF, Praveena T, Song H, Yoo JS, Jung DJ, Erturk-Hasdemir D, Hwang YS, Lee CC, Le Nours J, Kim H, Lee J, Blumberg RS, Rossjohn J, Park SB, Kasper DL Nature. 2021 Dec;600(7888):302-307. doi: 10.1038/s41586-021-04083-0. Epub 2021 , Nov 10. PMID:34759313<ref>PMID:34759313</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6xng" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Mus musculus]] |
| + | [[Category: Le Nours J]] | ||
| + | [[Category: Rossjohn J]] | ||
| + | [[Category: Thirunavukkarasu P]] | ||
Current revision
MHC-like protein complex structure
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