5eo8
From Proteopedia
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== 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> | ||
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| - | == Publication Abstract from PubMed == | ||
| - | The crystal structure of AOL (a fucose-specific lectin of Aspergillus oryzae) has been solved by SAD (single-wavelength anomalous diffraction) and MAD (multi-wavelength anomalous diffraction) phasing of seleno-fucosides. The overall structure is a six-bladed beta-propeller similar to that of other fucose-specific lectins. The fucose moieties of the seleno-fucosides are located in six fucose-binding sites. Although the Arg and Glu/Gln residues bound to the fucose moiety are common to all fucose-binding sites, the amino-acid residues involved in fucose binding at each site are not identical. The varying peak heights of the seleniums in the electron density map suggest that each fucose-binding site has a different carbohydrate binding affinity. | ||
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| - | Six independent fucose-binding sites in the crystal structure of Aspergillus oryzae lectin.,Makyio H, Shimabukuro J, Suzuki T, Imamura A, Ishida H, Kiso M, Ando H, Kato R Biochem Biophys Res Commun. 2016 Jun 16. pii: S0006-291X(16)30987-1. doi:, 10.1016/j.bbrc.2016.06.069. PMID:27318092<ref>PMID:27318092</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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| - | <div class="pdbe-citations 5eo8" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of AOL(868)
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