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3d5o
From Proteopedia
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==Structural recognition and functional activation of FcrR by innate pentraxins== | ==Structural recognition and functional activation of FcrR by innate pentraxins== | ||
| - | <StructureSection load='3d5o' size='340' side='right' caption='[[3d5o]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='3d5o' size='340' side='right'caption='[[3d5o]], [[Resolution|resolution]] 2.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3d5o]] is a 6 chain structure with sequence from [ | + | <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"><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> | + | </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 ([ | + | <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'>[ | + | <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> | </table> | ||
== Disease == | == 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 == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d5/3d5o_consurf.spt"</scriptWhenChecked> | + | <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> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3d5o" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3d5o" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Serum amyloid P-component|Serum amyloid P-component]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Clos, T W.Du]] | [[Category: Clos, T W.Du]] | ||
[[Category: Lu, J]] | [[Category: Lu, J]] | ||
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
