5h47
From Proteopedia
(Difference between revisions)
| Line 10: | Line 10: | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/LECF_ASPOR LECF_ASPOR] Lectin that specifically binds to L-fucose and weakly reacts with mannose and N-acetyl-neuraminic acid (PubMed:12092808, PubMed:27318092, PubMed:28041800). Has strongest preference for the alpha-1,6-fucosylated chain (core fucose) on glycoproteins among alpha-1,2-, alpha-1,3-, alpha-1,4-, and alpha-1,6-fucosylated chains (PubMed:17383961, PubMed:19109923). Binds to fucose residues of IgE in mice and human, causing antigen-independent IgE-mediated mast cell activation and anaphylactoid reactions in mice and is possibly implicated in allergic response to Aspergillus oryzae in humans (PubMed:21790704). Induces secretion of pro-inflammatory cytokines IL6 and IL8 implicated in ocular diseases such as mycotic keratitis, probably through its interaction with host toll-like receptors TLR2 and TLR4, followed by up-regulation of pro-inflammatory cytokines (PubMed:28470344).<ref>PMID:12092808</ref> <ref>PMID:17383961</ref> <ref>PMID:19109923</ref> <ref>PMID:21790704</ref> <ref>PMID:27318092</ref> <ref>PMID:28041800</ref> <ref>PMID:28470344</ref> | [https://www.uniprot.org/uniprot/LECF_ASPOR LECF_ASPOR] Lectin that specifically binds to L-fucose and weakly reacts with mannose and N-acetyl-neuraminic acid (PubMed:12092808, PubMed:27318092, PubMed:28041800). Has strongest preference for the alpha-1,6-fucosylated chain (core fucose) on glycoproteins among alpha-1,2-, alpha-1,3-, alpha-1,4-, and alpha-1,6-fucosylated chains (PubMed:17383961, PubMed:19109923). Binds to fucose residues of IgE in mice and human, causing antigen-independent IgE-mediated mast cell activation and anaphylactoid reactions in mice and is possibly implicated in allergic response to Aspergillus oryzae in humans (PubMed:21790704). Induces secretion of pro-inflammatory cytokines IL6 and IL8 implicated in ocular diseases such as mycotic keratitis, probably through its interaction with host toll-like receptors TLR2 and TLR4, followed by up-regulation of pro-inflammatory cytokines (PubMed:28470344).<ref>PMID:12092808</ref> <ref>PMID:17383961</ref> <ref>PMID:19109923</ref> <ref>PMID:21790704</ref> <ref>PMID:27318092</ref> <ref>PMID:28041800</ref> <ref>PMID:28470344</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Selenium-incorporated fucoses (seleno-fucoses) differing in the position of the seleno-substituent were synthesized and applied to the X-ray structural determination of a carbohydrate-lectin complex using single/multi-wavelength anomalous dispersion (SAD/MAD) phasing. The hydroxyl groups at the C-1, -2, -3 and -4 position of fucose were individually substituted with a methylseleno group via a transacetalization reaction using MeSeCH2OBn or by an SN2 reaction with TolSe- equivalents to afford the corresponding MeSe-fucose. The three-dimensional structures of a fucose-binding lectin complexed with several of these MeSe-fucoses have been determined by SAD/MAD phasing by utilizing the diffraction of selenium in the bound MeSe-fucoses. | ||
| - | |||
| - | Synthesis of seleno-fucose compounds and their application to the X-ray structural determination of carbohydrate-lectin complexes using single/multi-wavelength anomalous dispersion phasing.,Shimabukuro J, Makyio H, Suzuki T, Nishikawa Y, Kawasaki M, Imamura A, Ishida H, Ando H, Kato R, Kiso M Bioorg Med Chem. 2016 Dec 19. pii: S0968-0896(16)31172-5. doi:, 10.1016/j.bmc.2016.12.021. PMID:28041800<ref>PMID:28041800</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5h47" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of AOL complexed with 2-MeSe-Fuc
| |||||||||||
