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| | ==L-Ficolin Complexed to Phosphocholine== | | ==L-Ficolin Complexed to Phosphocholine== |
| - | <StructureSection load='4nyt' size='340' side='right' caption='[[4nyt]], [[Resolution|resolution]] 2.25Å' scene=''> | + | <StructureSection load='4nyt' size='340' side='right'caption='[[4nyt]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4nyt]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NYT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NYT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4nyt]] is a 3 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=4NYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NYT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PC:PHOSPHOCHOLINE'>PC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PC:PHOSPHOCHOLINE'>PC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j1g|2j1g]], [[2j0y|2j0y]], [[2j0g|2j0g]], [[2j2p|2j2p]], [[2j3f|2j3f]], [[2j0h|2j0h]], [[2j3g|2j3g]], [[2j3o|2j3o]], [[2j3u|2j3u]]</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=4nyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nyt OCA], [https://pdbe.org/4nyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nyt RCSB], [https://www.ebi.ac.uk/pdbsum/4nyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nyt ProSAT]</span></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=4nyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nyt OCA], [http://pdbe.org/4nyt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nyt RCSB], [http://www.ebi.ac.uk/pdbsum/4nyt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nyt ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FCN2_HUMAN FCN2_HUMAN]] May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin. Enhances phagocytosis of S.typhimurium by neutrophils, suggesting an opsonic effect via the collagen region.<ref>PMID:10679061</ref> | + | [https://www.uniprot.org/uniprot/FCN2_HUMAN FCN2_HUMAN] May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin. Enhances phagocytosis of S.typhimurium by neutrophils, suggesting an opsonic effect via the collagen region.<ref>PMID:10679061</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Gaboriaud, C]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Laffly, E]] | + | [[Category: Large Structures]] |
| - | [[Category: Martin, L]] | + | [[Category: Gaboriaud C]] |
| - | [[Category: Thielens, N]] | + | [[Category: Laffly E]] |
| - | [[Category: Extracellular]] | + | [[Category: Martin L]] |
| - | [[Category: Immune system]] | + | [[Category: Thielens N]] |
| - | [[Category: Soluble innate immune recognition]]
| + | |
| Structural highlights
4nyt is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
FCN2_HUMAN May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin. Enhances phagocytosis of S.typhimurium by neutrophils, suggesting an opsonic effect via the collagen region.[1]
Publication Abstract from PubMed
Human L-ficolin is a soluble protein of the innate immune system able to sense pathogens through its fibrinogen (FBG) recognition domains and to trigger activation of the lectin complement pathway through associated serine proteases. L-Ficolin has been previously shown to recognize pneumococcal clinical isolates, but its ligands and especially its molecular specificity remain to be identified. Using solid-phase binding assays, serum and recombinant L-ficolins were shown to interact with serotype 2 pneumococcal strain D39 and its unencapsulated R6 derivative. Incubation of both strains with serum triggered complement activation, as measured by C4b and C3b deposition, which was decreased by using ficolin-depleted serum. Recombinant L-ficolin and its FBG-like recognition domain bound to isolated pneumococcal cell wall extracts, whereas binding to cell walls depleted of teichoic acid (TA) was decreased. Both proteins were also shown to interact with two synthetic TA compounds, each comprising part structures of the complete lipoteichoic acid molecule with two PCho residues. Competition studies and direct interaction measurements by surface plasmon resonance identified PCho as a novel L-ficolin ligand. Structural analysis of complexes of the FBG domain of L-ficolin and PCho revealed that the phosphate moiety interacts with amino acids previously shown to define an acetyl binding site. Consequently, binding of L-ficolin to immobilized acetylated BSA was inhibited by PCho and synthetic TA. Binding of serum L-ficolin to immobilized synthetic TA and PCho-conjugated BSA triggered activation of the lectin complement pathway, thus further supporting the hypothesis of L-ficolin involvement in host antipneumococcal defense.
Human L-ficolin recognizes phosphocholine moieties of pneumococcal teichoic Acid.,Vassal-Stermann E, Lacroix M, Gout E, Laffly E, Pedersen CM, Martin L, Amoroso A, Schmidt RR, Zahringer U, Gaboriaud C, Di Guilmi AM, Thielens NM J Immunol. 2014 Dec 1;193(11):5699-708. doi: 10.4049/jimmunol.1400127. Epub 2014 , Oct 24. PMID:25344472[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Matsushita M, Endo Y, Fujita T. Cutting edge: complement-activating complex of ficolin and mannose-binding lectin-associated serine protease. J Immunol. 2000 Mar 1;164(5):2281-4. PMID:10679061
- ↑ Vassal-Stermann E, Lacroix M, Gout E, Laffly E, Pedersen CM, Martin L, Amoroso A, Schmidt RR, Zahringer U, Gaboriaud C, Di Guilmi AM, Thielens NM. Human L-ficolin recognizes phosphocholine moieties of pneumococcal teichoic Acid. J Immunol. 2014 Dec 1;193(11):5699-708. doi: 10.4049/jimmunol.1400127. Epub 2014 , Oct 24. PMID:25344472 doi:http://dx.doi.org/10.4049/jimmunol.1400127
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