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3d5o
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural recognition and functional activation of FcrR by innate pentraxins== | |
| + | <StructureSection load='3d5o' size='340' side='right'caption='[[3d5o]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3d5o]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D5O FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FCGR2A, CD32, FCG2, FCGR2A1, IGFR2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3d5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d5o OCA], [https://pdbe.org/3d5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d5o RCSB], [https://www.ebi.ac.uk/pdbsum/3d5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d5o ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[https://www.uniprot.org/uniprot/SAMP_HUMAN SAMP_HUMAN]] Note=SAP is a precursor of amyloid component P which is found in basement membrane and associated with amyloid deposits. | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/SAMP_HUMAN SAMP_HUMAN]] Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin. [[https://www.uniprot.org/uniprot/FCG2A_HUMAN FCG2A_HUMAN]] Binds to the Fc region of immunoglobulins gamma. Low affinity receptor. By binding to IgG it initiates cellular responses against pathogens and soluble antigens. Promotes phagocytosis of opsonized antigens.<ref>PMID:19011614</ref> | ||
| + | == 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/d5/3d5o_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=3d5o ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pentraxins are a family of ancient innate immune mediators conserved throughout evolution. The classical pentraxins include serum amyloid P component (SAP) and C-reactive protein, which are two of the acute-phase proteins synthesized in response to infection. Both recognize microbial pathogens and activate the classical complement pathway through C1q (refs 3 and 4). More recently, members of the pentraxin family were found to interact with cell-surface Fcgamma receptors (FcgammaR) and activate leukocyte-mediated phagocytosis. Here we describe the structural mechanism for pentraxin's binding to FcgammaR and its functional activation of FcgammaR-mediated phagocytosis and cytokine secretion. The complex structure between human SAP and FcgammaRIIa reveals a diagonally bound receptor on each SAP pentamer with both D1 and D2 domains of the receptor contacting the ridge helices from two SAP subunits. The 1:1 stoichiometry between SAP and FcgammaRIIa infers the requirement for multivalent pathogen binding for receptor aggregation. Mutational and binding studies show that pentraxins are diverse in their binding specificity for FcgammaR isoforms but conserved in their recognition structure. The shared binding site for SAP and IgG results in competition for FcgammaR binding and the inhibition of immune-complex-mediated phagocytosis by soluble pentraxins. These results establish antibody-like functions for pentraxins in the FcgammaR pathway, suggest an evolutionary overlap between the innate and adaptive immune systems, and have new therapeutic implications for autoimmune diseases. | ||
| - | + | Structural recognition and functional activation of FcgammaR by innate pentraxins.,Lu J, Marnell LL, Marjon KD, Mold C, Du Clos TW, Sun PD Nature. 2008 Dec 18;456(7224):989-92. Epub 2008 Nov 16. PMID:19011614<ref>PMID:19011614</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3d5o" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Serum amyloid P-component|Serum amyloid P-component]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Clos, T W.Du]] | ||
| + | [[Category: Lu, J]] | ||
| + | [[Category: Marjon, K D]] | ||
| + | [[Category: Marnell, L L]] | ||
| + | [[Category: Mold, C]] | ||
| + | [[Category: Sun, P D]] | ||
| + | [[Category: Amyloid]] | ||
| + | [[Category: Cell membrane]] | ||
| + | [[Category: Complex structure]] | ||
| + | [[Category: Fc receptor activation]] | ||
| + | [[Category: Fc riia]] | ||
| + | [[Category: Glycoprotein]] | ||
| + | [[Category: Igg-binding protein]] | ||
| + | [[Category: Immune system]] | ||
| + | [[Category: Immunoglobulin domain]] | ||
| + | [[Category: Lectin]] | ||
| + | [[Category: Membrane]] | ||
| + | [[Category: Metal-binding]] | ||
| + | [[Category: Pentraxin]] | ||
| + | [[Category: Phosphoprotein]] | ||
| + | [[Category: Receptor]] | ||
| + | [[Category: Sap]] | ||
| + | [[Category: Secreted]] | ||
| + | [[Category: Transmembrane]] | ||
Current revision
Structural recognition and functional activation of FcrR by innate pentraxins
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Categories: Human | Large Structures | Clos, T W.Du | Lu, J | Marjon, K D | Marnell, L L | Mold, C | Sun, P D | Amyloid | Cell membrane | Complex structure | Fc receptor activation | Fc riia | Glycoprotein | Igg-binding protein | Immune system | Immunoglobulin domain | Lectin | Membrane | Metal-binding | Pentraxin | Phosphoprotein | Receptor | Sap | Secreted | Transmembrane
