3m7o

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of mouse MD-1 in complex with phosphatidylcholine

Structural highlights

3m7o is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.65Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LY86_MOUSE May cooperate with CD180 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) and cytokine production. Important for efficient CD180 cell surface expression.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

MD-1 is a glycoprotein that associates with a B-cell-specific RP105 protein and has a low sequence identity of 16% to MD-2 that associates with Toll-like receptor 4 and recognizes endotoxic lipopolysaccharide. MD-1 and RP105 are supposed to mediate lipopolysaccharide recognition; however, little is known about their structures and functions. Here, the crystal structure of mouse MD-1 is determined at 1.65 A resolution. MD-1 has a hydrophobic cavity sandwiched by two beta-sheets as is MD-2. The cavity is 25 A long, 5 A wide, and 10 A deep: longer, narrower, and shallower than that of MD-2. No charged residues are located on the cavity entrance. MD-1 is primarily monomeric in solution but shows a dimeric assembly in the crystal lattices, with their cavity entrances facing each other. In the cavity, electron densities attributable to phosphatidylcholine are located. Together with the binding assay with tetra-acylated lipid IVa, MD-1 is shown to be a lipid-binding coreceptor.

Crystal structure of mouse MD-1 with endogenous phospholipid bound in its cavity.,Harada H, Ohto U, Satow Y J Mol Biol. 2010 Jul 23;400(4):838-46. Epub 2010 Jun 1. PMID:20595044^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gorczynski RM, Chen Z, Clark DA, Hu J, Yu G, Li X, Tsang W, Hadidi S. Regulation of gene expression of murine MD-1 regulates subsequent T cell activation and cytokine production. J Immunol. 2000 Aug 15;165(4):1925-32. PMID:10925274
↑ Harada H, Ohto U, Satow Y. Crystal structure of mouse MD-1 with endogenous phospholipid bound in its cavity. J Mol Biol. 2010 Jul 23;400(4):838-46. Epub 2010 Jun 1. PMID:20595044 doi:http://dx.doi.org/10.1016/j.jmb.2010.05.063

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3m7o"

Categories: Large Structures | Mus musculus | Harada H | Ohto U | Satow Y

@@ Line 1: / Line 1: @@
 ==Crystal structure of mouse MD-1 in complex with phosphatidylcholine==
-<StructureSection load='3m7o' size='340' side='right' caption='[[3m7o]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
+<StructureSection load='3m7o' size='340' side='right'caption='[[3m7o]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3m7o]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M7O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M7O FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3m7o]] 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=3M7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M7O FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=L9R:(2S)-3-(OCTADECANOYLOXY)-2-[(9Z)-OCTADEC-9-ENOYLOXY]PROPYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>L9R</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></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]] 1.65&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ly86, Md1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <scene name='pdbligand=L9R:(2S)-3-(OCTADECANOYLOXY)-2-[(9Z)-OCTADEC-9-ENOYLOXY]PROPYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>L9R</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3m7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m7o OCA], [http://pdbe.org/3m7o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m7o RCSB], [http://www.ebi.ac.uk/pdbsum/3m7o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m7o ProSAT]</span></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=3m7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m7o OCA], [https://pdbe.org/3m7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m7o RCSB], [https://www.ebi.ac.uk/pdbsum/3m7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m7o ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LY86_MOUSE LY86_MOUSE]] May cooperate with CD180 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) and cytokine production. Important for efficient CD180 cell surface expression.<ref>PMID:10925274</ref>
+[https://www.uniprot.org/uniprot/LY86_MOUSE LY86_MOUSE] May cooperate with CD180 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) and cytokine production. Important for efficient CD180 cell surface expression.<ref>PMID:10925274</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 15: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m7/3m7o_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Harada, H]]
+[[Category: Mus musculus]]
-[[Category: Ohto, U]]
+[[Category: Harada H]]
-[[Category: Satow, Y]]
+[[Category: Ohto U]]
-[[Category: Beta sheet]]
+[[Category: Satow Y]]
-[[Category: Glycoprotein]]
-[[Category: Immune system]]
-[[Category: Immunity]]
-[[Category: Inflammatory response]]
-[[Category: Innate immunity]]
-[[Category: Secreted]]

3m7o

From Proteopedia

Current revision

Crystal structure of mouse MD-1 in complex with phosphatidylcholine

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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