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| | <StructureSection load='5xrq' size='340' side='right'caption='[[5xrq]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='5xrq' size='340' side='right'caption='[[5xrq]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xrq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XRQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XRQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xrq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XRQ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xrs|5xrs]], [[5xrt|5xrt]], [[5w42|5w42]]</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]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DKFZp686P15220 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5xrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xrq OCA], [https://pdbe.org/5xrq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xrq RCSB], [https://www.ebi.ac.uk/pdbsum/5xrq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xrq 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=5xrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xrq OCA], [http://pdbe.org/5xrq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xrq RCSB], [http://www.ebi.ac.uk/pdbsum/5xrq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xrq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6N089_HUMAN Q6N089_HUMAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5xrq" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5xrq" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Willson, I A]] | + | [[Category: Willson IA]] |
| - | [[Category: Zhang, H]] | + | [[Category: Zhang H]] |
| - | [[Category: Antibody]]
| + | |
| - | [[Category: Fab]]
| + | |
| - | [[Category: Heavy chain]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Light chain]]
| + | |
| Structural highlights
Function
Q6N089_HUMAN
Publication Abstract from PubMed
The high rate of antigenic drift in seasonal influenza viruses necessitates frequent changes in vaccine composition. Recent seasonal H3 vaccines do not protect against swine-origin H3N2 variant (H3N2v) strains that recently have caused severe human infections. Here, we report a human VH1-69 gene-encoded monoclonal antibody (mAb) designated H3v-47 that exhibits potent cross-reactive neutralization activity against human and swine H3N2 viruses that circulated since 1989. The crystal structure and electron microscopy reconstruction of H3v-47 Fab with the H3N2v hemagglutinin (HA) identify a unique epitope spanning the vestigial esterase and receptor-binding subdomains that is distinct from that of any known neutralizing antibody for influenza A H3 viruses. MAb H3v-47 functions largely by blocking viral egress from infected cells. Interestingly, H3v-47 also engages Fcgamma receptor and mediates antibody dependent cellular cytotoxicity (ADCC). This newly identified conserved epitope can be used in design of novel immunogens for development of broadly protective H3 vaccines.
A multifunctional human monoclonal neutralizing antibody that targets a unique conserved epitope on influenza HA.,Bangaru S, Zhang H, Gilchuk IM, Voss TG, Irving RP, Gilchuk P, Matta P, Zhu X, Lang S, Nieusma T, Richt JA, Albrecht RA, Vanderven HA, Bombardi R, Kent SJ, Ward AB, Wilson IA, Crowe JE Jr Nat Commun. 2018 Jul 10;9(1):2669. doi: 10.1038/s41467-018-04704-9. PMID:29991715[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bangaru S, Zhang H, Gilchuk IM, Voss TG, Irving RP, Gilchuk P, Matta P, Zhu X, Lang S, Nieusma T, Richt JA, Albrecht RA, Vanderven HA, Bombardi R, Kent SJ, Ward AB, Wilson IA, Crowe JE Jr. A multifunctional human monoclonal neutralizing antibody that targets a unique conserved epitope on influenza HA. Nat Commun. 2018 Jul 10;9(1):2669. doi: 10.1038/s41467-018-04704-9. PMID:29991715 doi:http://dx.doi.org/10.1038/s41467-018-04704-9
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