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4d52

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CRYSTAL STRUCTURE OF FUCOSE BINDING LECTIN FROM ASPERGILLUS FUMIGATUS (AFL) IN COMPLEX WITH L-GALACTOPYRANOSE.

Structural highlights

4d52 is a 4 chain structure with sequence from Aspergillus fumigatus. This structure supersedes the now removed PDB entries 4uq7 and 4ahb. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.76Å
Ligands:	, , , , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2] ^[3] ^[4]

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kuboi S, Ishimaru T, Tamada S, Bernard EM, Perlin DS, Armstrong D. Molecular characterization of AfuFleA, an L-fucose-specific lectin from Aspergillus fumigatus. J Infect Chemother. 2013 Dec;19(6):1021-8. doi: 10.1007/s10156-013-0614-9. Epub, 2013 May 22. PMID:23695231 doi:http://dx.doi.org/10.1007/s10156-013-0614-9
↑ Houser J, Komarek J, Kostlanova N, Cioci G, Varrot A, Kerr SC, Lahmann M, Balloy V, Fahy JV, Chignard M, Imberty A, Wimmerova M. A Soluble Fucose-Specific Lectin from Aspergillus fumigatus Conidia - Structure, Specificity and Possible Role in Fungal Pathogenicity. PLoS One. 2013 Dec 10;8(12):e83077. doi: 10.1371/journal.pone.0083077. PMID:24340081 doi:http://dx.doi.org/10.1371/journal.pone.0083077
↑ Houser J, Komarek J, Cioci G, Varrot A, Imberty A, Wimmerova M. Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent. Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):442-53. doi:, 10.1107/S1399004714026595. Epub 2015 Feb 26. PMID:25760594 doi:http://dx.doi.org/10.1107/S1399004714026595
↑ Kerr SC, Fischer GJ, Sinha M, McCabe O, Palmer JM, Choera T, Lim FY, Wimmerova M, Carrington SD, Yuan S, Lowell CA, Oscarson S, Keller NP, Fahy JV. FleA Expression in Aspergillus fumigatus Is Recognized by Fucosylated Structures on Mucins and Macrophages to Prevent Lung Infection. PLoS Pathog. 2016 Apr 8;12(4):e1005555. doi: 10.1371/journal.ppat.1005555., eCollection 2016 Apr. PMID:27058347 doi:http://dx.doi.org/10.1371/journal.ppat.1005555
↑ Houser J, Komarek J, Cioci G, Varrot A, Imberty A, Wimmerova M. Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent. Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):442-53. doi:, 10.1107/S1399004714026595. Epub 2015 Feb 26. PMID:25760594 doi:http://dx.doi.org/10.1107/S1399004714026595

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4d52"

@@ Line 4: / Line 4: @@
 == 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='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>
+</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>
+[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 ==

4d52

From Proteopedia

Current revision

CRYSTAL STRUCTURE OF FUCOSE BINDING LECTIN FROM ASPERGILLUS FUMIGATUS (AFL) IN COMPLEX WITH L-GALACTOPYRANOSE.

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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