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| | <StructureSection load='4r9j' size='340' side='right'caption='[[4r9j]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='4r9j' size='340' side='right'caption='[[4r9j]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4r9j]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R9J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R9J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4r9j]] 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=4R9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R9J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3LJ:2-AMINO-2-DEOXY-6-O-SULFO-ALPHA-D-GLUCOPYRANOSE'>3LJ</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=3LJ:2-AMINO-2-DEOXY-6-O-SULFO-ALPHA-D-GLUCOPYRANOSE'>3LJ</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j0g|2j0g]], [[2j0h|2j0h]], [[2j0y|2j0y]], [[2j3o|2j3o]], [[4r9t|4r9t]]</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=4r9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r9j OCA], [https://pdbe.org/4r9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r9j RCSB], [https://www.ebi.ac.uk/pdbsum/4r9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r9j ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FCN2, FCNL ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r9j OCA], [http://pdbe.org/4r9j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r9j RCSB], [http://www.ebi.ac.uk/pdbsum/4r9j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r9j 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: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gaboriaud, C]] | + | [[Category: Gaboriaud C]] |
| - | [[Category: Lacroix, M]] | + | [[Category: Lacroix M]] |
| - | [[Category: Laffly, E]] | + | [[Category: Laffly E]] |
| - | [[Category: Martin, L]] | + | [[Category: Martin L]] |
| - | [[Category: Thielens, N]] | + | [[Category: Thielens N]] |
| - | [[Category: Vassal-Stermann, E]] | + | [[Category: Vassal-Stermann E]] |
| - | [[Category: Extracellular]]
| + | |
| - | [[Category: Fibrinogen-like domain]]
| + | |
| - | [[Category: Immunology]]
| + | |
| - | [[Category: Innate immunity]]
| + | |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Lectin-like]]
| + | |
| - | [[Category: Pattern recognition protein]]
| + | |
| - | [[Category: Plasma]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
4r9j 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
Ficolin-2 has been reported to bind to DNA and heparin, but the mechanism involved has not been thoroughly investigated. X-ray studies of the ficolin-2 fibrinogen-like domain in complex with several new ligands now show that sulfate and phosphate groups are prone to bind to the S3 binding site of the protein. Composed of Arg132, Asp133, Thr136 and Lys221, the S3 site was previously shown to mainly bind N-acetyl groups. Furthermore, DNA and heparin compete for binding to ficolin-2. Mutagenesis studies reveal that Arg132, and to a lesser extent Asp133, are important for this binding property. The versatility of the S3 site in binding N-acetyl, sulfate and phosphate groups is discussed through comparisons with homologous fibrinogen-like recognition proteins.
Human ficolin-2 recognition versatility extended: An update on the binding of ficolin-2 to sulfated/phosphated carbohydrates.,Laffly E, Lacroix M, Martin L, Vassal-Stermann E, Thielens NM, Gaboriaud C FEBS Lett. 2014 Dec 20;588(24):4694-700. doi: 10.1016/j.febslet.2014.10.042. Epub, 2014 Nov 11. PMID:25447524[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
- ↑ Laffly E, Lacroix M, Martin L, Vassal-Stermann E, Thielens NM, Gaboriaud C. Human ficolin-2 recognition versatility extended: An update on the binding of ficolin-2 to sulfated/phosphated carbohydrates. FEBS Lett. 2014 Dec 20;588(24):4694-700. doi: 10.1016/j.febslet.2014.10.042. Epub, 2014 Nov 11. PMID:25447524 doi:http://dx.doi.org/10.1016/j.febslet.2014.10.042
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