4d4u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:20, 20 December 2023) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal Structure of Fucose binding lectin from Aspergillus Fumigatus (AFL) in complex with LewisY tetrasaccharide.==
==Crystal Structure of Fucose binding lectin from Aspergillus Fumigatus (AFL) in complex with LewisY tetrasaccharide.==
-
<StructureSection load='4d4u' size='340' side='right' caption='[[4d4u]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
+
<StructureSection load='4d4u' size='340' side='right'caption='[[4d4u]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4d4u]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ah5 4ah5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D4U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D4U FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4d4u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ah5 4ah5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D4U FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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]] 1.99&#8491;</td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=PRD_900036:H+type+2+antigen,+beta+anomer'>PRD_900036</scene>, <scene name='pdbligand=PRD_900124:Lewis+Y+antigen,+alpha+anomer'>PRD_900124</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d52|4d52]]</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=4d4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d4u OCA], [https://pdbe.org/4d4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d4u RCSB], [https://www.ebi.ac.uk/pdbsum/4d4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d4u ProSAT]</span></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d4u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d4u RCSB], [http://www.ebi.ac.uk/pdbsum/4d4u PDBsum]</span></td></tr>
+
</table>
</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 4d4u" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Cioci, G]]
+
[[Category: Aspergillus fumigatus]]
-
[[Category: Houser, J]]
+
[[Category: Large Structures]]
-
[[Category: Imberty, A]]
+
[[Category: Cioci G]]
-
[[Category: Komarek, J]]
+
[[Category: Houser J]]
-
[[Category: Kostlanova, N]]
+
[[Category: Imberty A]]
-
[[Category: Lahmann, M]]
+
[[Category: Komarek J]]
-
[[Category: Varrot, A]]
+
[[Category: Kostlanova N]]
-
[[Category: Wimmerova, M]]
+
[[Category: Lahmann M]]
-
[[Category: Sugar binding protein]]
+
[[Category: Varrot A]]
 +
[[Category: Wimmerova M]]

Current revision

Crystal Structure of Fucose binding lectin from Aspergillus Fumigatus (AFL) in complex with LewisY tetrasaccharide.

PDB ID 4d4u

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools