2oya

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{{Seed}}
 
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[[Image:2oya.png|left|200px]]
 
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==Crystal structure analysis of the dimeric form of the SRCR domain of mouse MARCO==
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The line below this paragraph, containing "STRUCTURE_2oya", creates the "Structure Box" on the page.
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<StructureSection load='2oya' size='340' side='right'caption='[[2oya]], [[Resolution|resolution]] 1.77&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'>[[2oya]] 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=2OYA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OYA 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]] 1.77&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2oya| PDB=2oya | 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=2oya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oya OCA], [https://pdbe.org/2oya PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oya RCSB], [https://www.ebi.ac.uk/pdbsum/2oya PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oya ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MARCO_MOUSE MARCO_MOUSE] Pattern recognition receptor (PRR). Binds Gram-positive and Gram-negative bacteria.
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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/oy/2oya_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2oya 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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MARCO is a trimeric class A scavenger receptor of macrophages and dendritic cells that recognizes polyanionic particles and pathogens. The distal, scavenger receptor cysteine-rich (SRCR) domain of the extracellular part of this receptor has been implicated in ligand binding. To provide a structural basis for understanding the ligand-binding mechanisms of MARCO, we have determined the crystal structure of the mouse MARCO SRCR domain. The recombinant SRCR domain purified as monomeric and dimeric forms, and their structures were determined at 1.78 and 1.77 A resolution, respectively. The monomer has a compact globular fold with a twisted five-stranded antiparallel beta-sheet and a long loop covering a single alpha-helix, whereas the dimer is formed via beta-strand swapping of two monomers, thus containing a large eight-stranded beta-sheet. Calculation of the surface electrostatic potential revealed that the beta-sheet region with several arginines forms a basic cluster. Unexpectedly, an acidic cluster was found in the long loop region. In the monomer, the acidic cluster is involved in metal ion binding. Studies with cells expressing various SRCR domain mutants showed that all of the arginines of the basic cluster are involved in ligand binding, suggesting a cooperative binding mechanism. Ligand binding is also dependent on the acidic cluster and Ca2+ ions whose depletion appears to affect ligand binding at least by modulating the electrostatic potential or relative domain orientation. We propose that the SRCR domain dimerization can contribute to the recognition of large ligands by providing a means for the MARCO receptor oligomerization.
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===Crystal structure analysis of the dimeric form of the SRCR domain of mouse MARCO===
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Crystal structure of the cysteine-rich domain of scavenger receptor MARCO reveals the presence of a basic and an acidic cluster that both contribute to ligand recognition.,Ojala JR, Pikkarainen T, Tuuttila A, Sandalova T, Tryggvason K J Biol Chem. 2007 Jun 1;282(22):16654-66. Epub 2007 Apr 3. PMID:17405873<ref>PMID:17405873</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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The line below this paragraph, {{ABSTRACT_PUBMED_17405873}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2oya" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17405873 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17405873}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2OYA is a 2 chains structure of 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=2OYA OCA].
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==Reference==
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<ref group="xtra">PMID:17405873</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Ojala, J R.M.]]
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[[Category: Ojala JRM]]
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[[Category: Pikkarainen, T.]]
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[[Category: Pikkarainen T]]
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[[Category: Sandalova, T.]]
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[[Category: Sandalova T]]
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[[Category: Tryggvason, K.]]
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[[Category: Tryggvason K]]
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[[Category: Tuuttila, A.]]
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[[Category: Tuuttila A]]
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[[Category: Acidic cluster]]
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[[Category: Basic cluster]]
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[[Category: Dimer]]
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[[Category: Extracellular matrix]]
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[[Category: Ligand binding]]
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[[Category: Macrophage receptor]]
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[[Category: Sulfate binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 10:29:16 2009''
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Current revision

Crystal structure analysis of the dimeric form of the SRCR domain of mouse MARCO

PDB ID 2oya

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