3ilq

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{{Seed}}
 
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[[Image:3ilq.png|left|200px]]
 
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==Structure of mCD1d with bound glycolipid BbGL-2c from Borrelia burgdorferi==
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The line below this paragraph, containing "STRUCTURE_3ilq", creates the "Structure Box" on the page.
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<StructureSection load='3ilq' size='340' side='right'caption='[[3ilq]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3ilq]] is a 2 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=3ILQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ILQ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1O2:(2S)-3-(ALPHA-D-GALACTOPYRANOSYLOXY)-2-(HEXADECANOYLOXY)PROPYL+(9Z)-OCTADEC-9-ENOATE'>1O2</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_3ilq| PDB=3ilq | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ilq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ilq OCA], [https://pdbe.org/3ilq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ilq RCSB], [https://www.ebi.ac.uk/pdbsum/3ilq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ilq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/3ilq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ilq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Invariant natural killer T cells (iNKT cells) respond to CD1d-presented glycolipids from Borrelia burgdorferi, the causative agent of Lyme disease. Although mouse and human iNKT cells respond to different antigens based on subtle differences in their fatty acids, the mechanism by which fatty acid structure determines antigenic potency is not well understood. Here we show that the mouse and human CD1d present glycolipids having different fatty acids, based in part upon a difference at a single amino acid position that is involved in positioning the sugar epitope. CD1d also can bind nonantigenic lipids, however, but unexpectedly, mouse CD1d orients the two aliphatic chains of a nonantigenic lipid rotated 180 degrees , causing a dramatic repositioning of the exposed sugar. Therefore, our data reveal the biochemical basis for the high degree of antigenic specificity of iNKT cells for certain fatty acids, and they suggest how microbes could alter fatty acid biosynthesis as an immune evasion mechanism.
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===Structure of mCD1d with bound glycolipid BbGL-2c from Borrelia burgdorferi===
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Lipid binding orientation within CD1d affects recognition of Borrelia burgorferi antigens by NKT cells.,Wang J, Li Y, Kinjo Y, Mac TT, Gibson D, Painter GF, Kronenberg M, Zajonc DM Proc Natl Acad Sci U S A. 2009 Dec 30. PMID:20080535<ref>PMID:20080535</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ilq" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20080535}}, adds the Publication Abstract to the page
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*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20080535 is the PubMed ID number.
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*[[CD1|CD1]]
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== References ==
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{{ABSTRACT_PUBMED_20080535}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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3ILQ is a 2 chains structure with sequences 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=3ILQ OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:20080535</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Zajonc, D M.]]
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[[Category: Zajonc DM]]
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[[Category: Antigen presentation]]
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[[Category: Borrelia burgdorferi]]
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[[Category: Cd1]]
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[[Category: Cell membrane]]
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[[Category: Disulfide bond]]
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[[Category: Endosome]]
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[[Category: Glycoprotein]]
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[[Category: Host defense]]
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[[Category: Immune response]]
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[[Category: Immune system]]
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[[Category: Immunoglobulin domain]]
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[[Category: Inkt cell]]
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[[Category: Innate immunity]]
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[[Category: Lysosome]]
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[[Category: Membrane]]
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[[Category: Mhc i]]
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[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 3 14:24:26 2010''
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Current revision

Structure of mCD1d with bound glycolipid BbGL-2c from Borrelia burgdorferi

PDB ID 3ilq

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