7kf9: Difference between revisions
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==== | ==Ebola virus GP (mucin deleted, Makona strain) bound to antibody Fab EBOV-296 and EBOV-515== | ||
<StructureSection load='7kf9' size='340' side='right'caption='[[7kf9]]' scene=''> | <StructureSection load='7kf9' size='340' side='right'caption='[[7kf9]], [[Resolution|resolution]] 4.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7kf9]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Ebola_virus Ebola virus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KF9 FirstGlance]. <br> | ||
</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=7kf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kf9 OCA], [https://pdbe.org/7kf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kf9 RCSB], [https://www.ebi.ac.uk/pdbsum/7kf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kf9 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.4Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=7kf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kf9 OCA], [https://pdbe.org/7kf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kf9 RCSB], [https://www.ebi.ac.uk/pdbsum/7kf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kf9 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Antibodies that target the glycan cap epitope on the ebolavirus glycoprotein (GP) are common in the adaptive response of survivors. A subset is known to be broadly neutralizing, but the details of their epitopes and basis for neutralization are not well understood. Here, we present cryoelectron microscopy (cryo-EM) structures of diverse glycan cap antibodies that variably synergize with GP base-binding antibodies. These structures describe a conserved site of vulnerability that anchors the mucin-like domains (MLDs) to the glycan cap, which we call the MLD anchor and cradle. Antibodies that bind to the MLD cradle share common features, including use of IGHV1-69 and IGHJ6 germline genes, which exploit hydrophobic residues and form beta-hairpin structures to mimic the MLD anchor, disrupt MLD attachment, destabilize GP quaternary structure, and block cleavage events required for receptor binding. Our results provide a molecular basis for ebolavirus neutralization by broadly reactive glycan cap antibodies. | |||
Convergence of a common solution for broad ebolavirus neutralization by glycan cap-directed human antibodies.,Murin CD, Gilchuk P, Ilinykh PA, Huang K, Kuzmina N, Shen X, Bruhn JF, Bryan AL, Davidson E, Doranz BJ, Williamson LE, Copps J, Alkutkar T, Flyak AI, Bukreyev A, Crowe JE Jr, Ward AB Cell Rep. 2021 Apr 13;35(2):108984. doi: 10.1016/j.celrep.2021.108984. PMID:33852862<ref>PMID:33852862</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7kf9" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ebola virus]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Murin CD]] | ||
[[Category: Ward AB]] | |||
Latest revision as of 11:55, 17 October 2024
Ebola virus GP (mucin deleted, Makona strain) bound to antibody Fab EBOV-296 and EBOV-515Ebola virus GP (mucin deleted, Makona strain) bound to antibody Fab EBOV-296 and EBOV-515
Structural highlights
Publication Abstract from PubMedAntibodies that target the glycan cap epitope on the ebolavirus glycoprotein (GP) are common in the adaptive response of survivors. A subset is known to be broadly neutralizing, but the details of their epitopes and basis for neutralization are not well understood. Here, we present cryoelectron microscopy (cryo-EM) structures of diverse glycan cap antibodies that variably synergize with GP base-binding antibodies. These structures describe a conserved site of vulnerability that anchors the mucin-like domains (MLDs) to the glycan cap, which we call the MLD anchor and cradle. Antibodies that bind to the MLD cradle share common features, including use of IGHV1-69 and IGHJ6 germline genes, which exploit hydrophobic residues and form beta-hairpin structures to mimic the MLD anchor, disrupt MLD attachment, destabilize GP quaternary structure, and block cleavage events required for receptor binding. Our results provide a molecular basis for ebolavirus neutralization by broadly reactive glycan cap antibodies. Convergence of a common solution for broad ebolavirus neutralization by glycan cap-directed human antibodies.,Murin CD, Gilchuk P, Ilinykh PA, Huang K, Kuzmina N, Shen X, Bruhn JF, Bryan AL, Davidson E, Doranz BJ, Williamson LE, Copps J, Alkutkar T, Flyak AI, Bukreyev A, Crowe JE Jr, Ward AB Cell Rep. 2021 Apr 13;35(2):108984. doi: 10.1016/j.celrep.2021.108984. PMID:33852862[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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