4aha
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4aha is ON HOLD Authors: Houser, J., Komarek, J., Kostlanova, N., Lahmann, M., Cioci, G., Varrot, A., Imberty, A., Wimmerova, M. Description: Cryst...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Fucose binding lectin from Aspergillus Fumigatus (AFL) in complex with fucosylated monosaccharides (Fuc1-2Gal, Fuc1- 3GlcNAc, Fuc1-4GlcNAc and Fuc1-6GlcNAc)== | |
| + | <StructureSection load='4aha' size='340' side='right'caption='[[4aha]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4aha]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AHA FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4aha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aha OCA], [https://pdbe.org/4aha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aha RCSB], [https://www.ebi.ac.uk/pdbsum/4aha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aha ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LECF_ASPFU LECF_ASPFU] Multispecific lectin that is able to recognize L-fucose in all possible linkages (PubMed:23695231, PubMed:27058347, PubMed:24340081, PubMed:25760594). These could be found not only in decomposed plant matter in soil, which is the natural environment for A.fumigatus, but also in various epitopes on human tissues (PubMed:25760594). Mediates binding of A.fumigatus conidia to airway mucinin a fucose dependent manner (PubMed:27058347). Stimulates IL-8 production by human bronchial cells in a dose-dependent manner, contributing to the inflammatory response observed upon the exposure of a patient to A.fumigatus, and thus might be an important virulence factor involved in an early stage of A.fumigatus infection (PubMed:24340081).<ref>PMID:23695231</ref> <ref>PMID:24340081</ref> <ref>PMID:25760594</ref> <ref>PMID:27058347</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Aspergillus fumigatus lectin AFL was recently described as a new member of the AAL lectin family. As a lectin from an opportunistic pathogen, it might play an important role in the interaction of the pathogen with the human host. A detailed study of structures of AFL complexed with several monosaccharides and oligosaccharides, including blood-group epitopes, was combined with affinity data from SPR and discussed in the context of previous findings. Its six binding sites are non-equivalent, and owing to minor differences in amino-acid composition they exhibit a marked difference in specific ligand recognition. AFL displays a high affinity in the micromolar range towards oligosaccharides which were detected in plants and also those bound on the human epithelia. All of these results indicate AFL to be a complex member of the lectin family and a challenging target for future medical research and, owing to its binding properties, a potentially useful tool in specific biotechnological applications. | ||
| - | + | Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent.,Houser J, Komarek J, Cioci G, Varrot A, Imberty A, Wimmerova M Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):442-53. doi:, 10.1107/S1399004714026595. Epub 2015 Feb 26. PMID:25760594<ref>PMID:25760594</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4aha" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspergillus fumigatus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cioci G]] | ||
| + | [[Category: Houser J]] | ||
| + | [[Category: Imberty A]] | ||
| + | [[Category: Komarek J]] | ||
| + | [[Category: Kostlanova N]] | ||
| + | [[Category: Lahmann M]] | ||
| + | [[Category: Varrot A]] | ||
| + | [[Category: Wimmerova M]] | ||
Current revision
Crystal Structure of Fucose binding lectin from Aspergillus Fumigatus (AFL) in complex with fucosylated monosaccharides (Fuc1-2Gal, Fuc1- 3GlcNAc, Fuc1-4GlcNAc and Fuc1-6GlcNAc)
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