6u1t: Difference between revisions

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<StructureSection load='6u1t' size='340' side='right'caption='[[6u1t]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
<StructureSection load='6u1t' size='340' side='right'caption='[[6u1t]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6u1t]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U1T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6U1T FirstGlance]. <br>
<table><tr><td colspan='2'>[[6u1t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U1T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6U1T FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6tys|6tys]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6tys|6tys]]</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=6u1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u1t OCA], [http://pdbe.org/6u1t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u1t RCSB], [http://www.ebi.ac.uk/pdbsum/6u1t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u1t 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=6u1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u1t OCA], [http://pdbe.org/6u1t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u1t RCSB], [http://www.ebi.ac.uk/pdbsum/6u1t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u1t ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nipah virus (NiV) and Hendra virus (HeV) are zoonotic henipaviruses (HNVs) responsible for outbreaks of encephalitis and respiratory illness with fatality rates of 50-100%. No vaccines or licensed therapeutics currently exist to protect humans against NiV or HeV. HNVs enter host cells by fusing the viral and cellular membranes via the concerted action of the attachment (G) and fusion (F) glycoproteins, the main targets of the humoral immune response. Here, we describe the isolation and humanization of a potent monoclonal antibody cross-neutralizing NiV and HeV. Cryo-electron microscopy, triggering and fusion studies show the antibody binds to a prefusion-specific quaternary epitope, conserved in NiV F and HeV F glycoproteins, and prevents membrane fusion and viral entry. This work supports the importance of the HNV prefusion F conformation for eliciting a robust immune response and paves the way for using this antibody for prophylaxis and post-exposure therapy with NiV- and HeV-infected individuals.
An antibody against the F glycoprotein inhibits Nipah and Hendra virus infections.,Dang HV, Chan YP, Park YJ, Snijder J, Da Silva SC, Vu B, Yan L, Feng YR, Rockx B, Geisbert TW, Mire CE, Broder CC, Veesler D Nat Struct Mol Biol. 2019 Sep 30. pii: 10.1038/s41594-019-0308-9. doi:, 10.1038/s41594-019-0308-9. PMID:31570878<ref>PMID:31570878</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6u1t" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: BBroder, C C]]
[[Category: BBroder, C C]]
[[Category: Chan, Y P]]
[[Category: Chan, Y P]]

Revision as of 14:52, 13 November 2019

Crystal structure of anti-Nipah virus (NiV) F 5B3 antibody Fab fragmentCrystal structure of anti-Nipah virus (NiV) F 5B3 antibody Fab fragment

Structural highlights

6u1t is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Nipah virus (NiV) and Hendra virus (HeV) are zoonotic henipaviruses (HNVs) responsible for outbreaks of encephalitis and respiratory illness with fatality rates of 50-100%. No vaccines or licensed therapeutics currently exist to protect humans against NiV or HeV. HNVs enter host cells by fusing the viral and cellular membranes via the concerted action of the attachment (G) and fusion (F) glycoproteins, the main targets of the humoral immune response. Here, we describe the isolation and humanization of a potent monoclonal antibody cross-neutralizing NiV and HeV. Cryo-electron microscopy, triggering and fusion studies show the antibody binds to a prefusion-specific quaternary epitope, conserved in NiV F and HeV F glycoproteins, and prevents membrane fusion and viral entry. This work supports the importance of the HNV prefusion F conformation for eliciting a robust immune response and paves the way for using this antibody for prophylaxis and post-exposure therapy with NiV- and HeV-infected individuals.

An antibody against the F glycoprotein inhibits Nipah and Hendra virus infections.,Dang HV, Chan YP, Park YJ, Snijder J, Da Silva SC, Vu B, Yan L, Feng YR, Rockx B, Geisbert TW, Mire CE, Broder CC, Veesler D Nat Struct Mol Biol. 2019 Sep 30. pii: 10.1038/s41594-019-0308-9. doi:, 10.1038/s41594-019-0308-9. PMID:31570878[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Dang HV, Chan YP, Park YJ, Snijder J, Da Silva SC, Vu B, Yan L, Feng YR, Rockx B, Geisbert TW, Mire CE, Broder CC, Veesler D. An antibody against the F glycoprotein inhibits Nipah and Hendra virus infections. Nat Struct Mol Biol. 2019 Sep 30. pii: 10.1038/s41594-019-0308-9. doi:, 10.1038/s41594-019-0308-9. PMID:31570878 doi:http://dx.doi.org/10.1038/s41594-019-0308-9

6u1t, resolution 1.48Å

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OCA