4wen
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4wen is ON HOLD until Paper Publication Authors: Moonens, K., Van den Broeck, I., Pardon, E., De Kerpel, M., Remaut, H., De Greve, H. Description: ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Co-complex structure of the F4 fimbrial adhesin FaeG variant ac with llama single domain antibody V2== | |
| + | <StructureSection load='4wen' size='340' side='right'caption='[[4wen]], [[Resolution|resolution]] 1.89Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4wen]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WEN 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]] 1.89Å</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=4wen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wen OCA], [https://pdbe.org/4wen PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wen RCSB], [https://www.ebi.ac.uk/pdbsum/4wen PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wen ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FAEG2_ECOLX FAEG2_ECOLX] K88 major fimbrial subunit. Fimbriae (also called pili), are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell. They enable bacteria to colonize the epithelium of specific host organs. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Enterotoxigenic Escherichia coli that cause neonatal and post-weaning diarrhea in piglets express F4 fimbriae to mediate attachment towards host receptors. Recently we described how llama single domain antibodies (VHHs) fused to IgA, produced in Arabidopsis thaliana seeds and fed to piglets resulted in a progressive decline in shedding of F4 positive ETEC bacteria. Here we present the structures of these inhibiting VHHs in complex with the major adhesive subunit FaeG. A conserved surface, distant from the lactose binding pocket, is targeted by these VHHs, highlighting the possibility of targeting epitopes on single-domain adhesins that are non-involved in receptor binding. | ||
| - | + | Structural insight in the inhibition of adherence of F4 fimbriae producing enterotoxigenic Escherichia coli by llama single domain antibodies.,Moonens K, Van den Broeck I, Okello E, Pardon E, De Kerpel M, Remaut H, De Greve H Vet Res. 2015 Feb 24;46(1):14. doi: 10.1186/s13567-015-0151-x. PMID:25828907<ref>PMID:25828907</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4wen" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Antibody 3D structures|Antibody 3D structures]] | ||
| + | *[[Pilin 3D structures|Pilin 3D structures]] | ||
| + | *[[3D structures of non-human antibody|3D structures of non-human antibody]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Lama glama]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: De Greve H]] | ||
| + | [[Category: De Kerpel M]] | ||
| + | [[Category: Moonens K]] | ||
| + | [[Category: Pardon E]] | ||
| + | [[Category: Remaut H]] | ||
| + | [[Category: Van den Broeck I]] | ||
Current revision
Co-complex structure of the F4 fimbrial adhesin FaeG variant ac with llama single domain antibody V2
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