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2e59
From Proteopedia
(Difference between revisions)
(New page: 200px<br /> <applet load="2e59" size="450" color="white" frame="true" align="right" spinBox="true" caption="2e59, resolution 2.21Å" /> '''Crystal structure o...) |
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| - | [[Image:2e59.gif|left|200px]]<br /> | ||
| - | <applet load="2e59" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2e59, resolution 2.21Å" /> | ||
| - | '''Crystal structure of human MD-2 in complex with lipid IVa'''<br /> | ||
| - | == | + | ==Crystal structure of human MD-2 in complex with lipid IVa== |
| - | + | <StructureSection load='2e59' size='340' side='right'caption='[[2e59]], [[Resolution|resolution]] 2.21Å' scene=''> | |
| - | [[ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[2e59]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E59 FirstGlance]. <br> |
| - | [[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21Å</td></tr> |
| - | [[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LP4:2-DEOXY-3-O-[(3R)-3-HYDROXYTETRADECANOYL]-2-{[(3R)-3-HYDROXYTETRADECANOYL]AMINO}-4-O-PHOSPHONO-BETA-D-GLUCOPYRANOSE'>LP4</scene>, <scene name='pdbligand=LP5:(R)-((2R,3S,4R,5R,6R)-3-HYDROXY-2-(HYDROXYMETHYL)-5-((R)-3-HYDROXYTETRADECANAMIDO)-6-(PHOSPHONOOXY)TETRAHYDRO-2H-PYRAN-4-YL)+3-HYDROXYTETRADECANOATE'>LP5</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'>[https://proteopedia.org/fgij/fg.htm?mol=2e59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e59 OCA], [https://pdbe.org/2e59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e59 RCSB], [https://www.ebi.ac.uk/pdbsum/2e59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e59 ProSAT]</span></td></tr> |
| - | [[ | + | </table> |
| - | [ | + | == Function == |
| - | [[ | + | [https://www.uniprot.org/uniprot/LY96_HUMAN LY96_HUMAN] Cooperates with TLR4 in the innate immune response to bacterial lipopolysaccharide (LPS), and with TLR2 in the response to cell wall components from Gram-positive and Gram-negative bacteria. Enhances TLR4-dependent activation of NF-kappa-B. Cells expressing both MD2 and TLR4, but not TLR4 alone, respond to LPS. |
| - | + | == Evolutionary Conservation == | |
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e5/2e59_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2e59 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Endotoxic lipopolysaccharide (LPS) with potent immunostimulatory activity is recognized by the receptor complex of MD-2 and Toll-like receptor 4. Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively. MD-2 shows a deep hydrophobic cavity sandwiched by two beta sheets, in which four acyl chains of the ligand are fully confined. The phosphorylated glucosamine moieties are located at the entrance to the cavity. These structures suggest that MD-2 plays a principal role in endotoxin recognition and provide a basis for antiseptic drug development. | ||
| - | + | Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa.,Ohto U, Fukase K, Miyake K, Satow Y Science. 2007 Jun 15;316(5831):1632-4. PMID:17569869<ref>PMID:17569869</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2e59" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ohto U]] | ||
| + | [[Category: Satow Y]] | ||
Current revision
Crystal structure of human MD-2 in complex with lipid IVa
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