7m72: Difference between revisions

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====
==MHC-like protein complex structure==
<StructureSection load='7m72' size='340' side='right'caption='[[7m72]]' scene=''>
<StructureSection load='7m72' size='340' side='right'caption='[[7m72]], [[Resolution|resolution]] 2.40&Aring;' 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'>[[7m72]] 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=7M72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M72 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=7m72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m72 OCA], [https://pdbe.org/7m72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m72 RCSB], [https://www.ebi.ac.uk/pdbsum/7m72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m72 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]] 2.4&#8491;</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=HP6:HEPTANE'>HP6</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=QOD:(3R)-N-[(2S,3R)-1-(alpha-D-galactopyranosyloxy)-3-hydroxy-15-methylhexadecan-2-yl]-3-hydroxyheptadecanamide'>QOD</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=7m72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m72 OCA], [https://pdbe.org/7m72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m72 RCSB], [https://www.ebi.ac.uk/pdbsum/7m72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m72 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7m72" style="background-color:#fffaf0;"></div>
==See Also==
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
*[[CD1|CD1]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Z-disk]]
[[Category: Mus musculus]]
[[Category: Le Nours J]]
[[Category: Rossjohn J]]
[[Category: Thirunavukkarasu P]]

Revision as of 16:06, 18 October 2023

MHC-like protein complex structure

7m72, resolution 2.40Å

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