7cab: Difference between revisions
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<StructureSection load='7cab' size='340' side='right'caption='[[7cab]], [[Resolution|resolution]] 3.52Å' scene=''> | <StructureSection load='7cab' size='340' side='right'caption='[[7cab]], [[Resolution|resolution]] 3.52Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CAB FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.52Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=7cab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cab OCA], [https://pdbe.org/7cab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cab RCSB], [https://www.ebi.ac.uk/pdbsum/7cab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cab ProSAT]</span></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=7cab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cab OCA], [https://pdbe.org/7cab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cab RCSB], [https://www.ebi.ac.uk/pdbsum/7cab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cab ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<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 7cab" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7cab" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cao | [[Category: Cao L]] | ||
[[Category: Deng | [[Category: Deng Y]] | ||
[[Category: Qin | [[Category: Qin C]] | ||
[[Category: Rao | [[Category: Rao Z]] | ||
[[Category: Sun | [[Category: Sun Y]] | ||
[[Category: Wang | [[Category: Wang N]] | ||
[[Category: Wang | [[Category: Wang X]] | ||
[[Category: Wang | [[Category: Wang Y]] | ||
[[Category: Xie | [[Category: Xie L]] | ||
[[Category: Zhe | [[Category: Zhe L]] | ||
Latest revision as of 11:38, 17 October 2024
Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibodyStructural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody
Structural highlights
Publication Abstract from PubMedThe coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has resulted in an unprecedented public health crisis. There are no approved vaccines or therapeutics for treating COVID-19. Here we report a humanized monoclonal antibody, H014, that efficiently neutralizes SARS-CoV-2 and SARS-CoV pseudoviruses as well as authentic SARS-CoV-2 at nanomolar concentrations by engaging the spike (S) receptor binding domain (RBD). H014 administration reduced SARS-CoV-2 titers in infected lungs and prevented pulmonary pathology in a human angiotensin-converting enzyme 2 mouse model. Cryo-electron microscopy characterization of the SARS-CoV-2 S trimer in complex with the H014 Fab fragment unveiled a previously uncharacterized conformational epitope, which was only accessible when the RBD was in an open conformation. Biochemical, cellular, virological, and structural studies demonstrated that H014 prevents attachment of SARS-CoV-2 to its host cell receptors. Epitope analysis of available neutralizing antibodies against SARS-CoV and SARS-CoV-2 uncovered broad cross-protective epitopes. Our results highlight a key role for antibody-based therapeutic interventions in the treatment of COVID-19. Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody.,Lv Z, Deng YQ, Ye Q, Cao L, Sun CY, Fan C, Huang W, Sun S, Sun Y, Zhu L, Chen Q, Wang N, Nie J, Cui Z, Zhu D, Shaw N, Li XF, Li Q, Xie L, Wang Y, Rao Z, Qin CF, Wang X Science. 2020 Sep 18;369(6510):1505-1509. doi: 10.1126/science.abc5881. Epub 2020, Jul 23. PMID:32703908[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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