View source for 6vy4


==Crystal structure of Hendra receptor binding protein head domain in complex with human neutralizing antibody HENV-32==
<StructureSection load='6vy4' size='340' side='right'caption='[[6vy4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6vy4]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Henipavirus_hendraense Henipavirus hendraense] 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=6VY4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VY4 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6vy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vy4 OCA], [https://pdbe.org/6vy4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vy4 RCSB], [https://www.ebi.ac.uk/pdbsum/6vy4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vy4 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Hendra (HeV) and Nipah (NiV) viruses are emerging zoonotic pathogens in the Henipavirus genus causing outbreaks of disease with very high case fatality rates. Here, we report the first naturally occurring human monoclonal antibodies (mAbs) against HeV receptor binding protein (RBP). All isolated mAbs neutralized HeV, and some also neutralized NiV. Epitope binning experiments identified five major antigenic sites on HeV-RBP. Animal studies demonstrated that the most potent cross-reactive neutralizing mAbs, HENV-26 and HENV-32, protected ferrets in lethal models of infection with NiV Bangladesh 3 days after exposure. We solved the crystal structures of mAb HENV-26 in complex with both HeV-RBP and NiV-RBP and of mAb HENV-32 in complex with HeV-RBP. The studies reveal diverse sites of vulnerability on RBP recognized by potent human mAbs that inhibit virus by multiple mechanisms. These studies identify promising prophylactic antibodies and define protective epitopes that can be used in rational vaccine design.

Potent Henipavirus Neutralization by Antibodies Recognizing Diverse Sites on Hendra and Nipah Virus Receptor Binding Protein.,Dong J, Cross RW, Doyle MP, Kose N, Mousa JJ, Annand EJ, Borisevich V, Agans KN, Sutton R, Nargi R, Majedi M, Fenton KA, Reichard W, Bombardi RG, Geisbert TW, Crowe JE Jr Cell. 2020 Dec 10;183(6):1536-1550.e17. doi: 10.1016/j.cell.2020.11.023. PMID:33306954<ref>PMID:33306954</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6vy4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Henipavirus hendraense]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Crowe JE]]
[[Category: Dong J]]