View source for 4d52


==CRYSTAL STRUCTURE OF FUCOSE BINDING LECTIN FROM ASPERGILLUS FUMIGATUS (AFL) IN COMPLEX WITH L-GALACTOPYRANOSE.==
<StructureSection load='4d52' size='340' side='right'caption='[[4d52]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4d52]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4uq7 4uq7] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ahb 4ahb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D52 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]] 1.76&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=GIV:BETA-L-GALACTOPYRANOSE'>GIV</scene>, <scene name='pdbligand=GXL:ALPHA-L-GALACTOPYRANOSE'>GXL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4d52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d52 OCA], [https://pdbe.org/4d52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d52 RCSB], [https://www.ebi.ac.uk/pdbsum/4d52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d52 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4d52" 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: Wimmerowa M]]