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4r9t
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4r9t is ON HOLD Authors: Laffly, E., Lacroix, M., Martin, L., Vassal-Stermann, E., Thielens, N., Gaboriaud, C. Description: L-ficolin complexed to ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==L-ficolin complexed to sulphates== | |
| + | <StructureSection load='4r9t' size='340' side='right'caption='[[4r9t]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4r9t]] 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=4R9T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R9T FirstGlance]. <br> | ||
| + | </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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4r9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r9t OCA], [https://pdbe.org/4r9t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r9t RCSB], [https://www.ebi.ac.uk/pdbsum/4r9t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r9t ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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;"> | ||
| + | == 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<ref>PMID:25447524</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4r9t" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ficolin|Ficolin]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gaboriaud C]] | ||
| + | [[Category: Lacroix M]] | ||
| + | [[Category: Laffly E]] | ||
| + | [[Category: Martin L]] | ||
| + | [[Category: Thielens N]] | ||
| + | [[Category: Vassal-Stermann E]] | ||
Current revision
L-ficolin complexed to sulphates
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