7u9g: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7u9g]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rabies_virus_strain_Pasteur_vaccin Rabies virus strain Pasteur vaccin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7U9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7U9G FirstGlance]. <br> | <table><tr><td colspan='2'>[[7u9g]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rabies_virus_strain_Pasteur_vaccin Rabies virus strain Pasteur vaccin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7U9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7U9G FirstGlance]. <br> | ||
</td></tr><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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.39Å</td></tr> | ||
<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=7u9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7u9g OCA], [https://pdbe.org/7u9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7u9g RCSB], [https://www.ebi.ac.uk/pdbsum/7u9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7u9g 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=7u9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7u9g OCA], [https://pdbe.org/7u9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7u9g RCSB], [https://www.ebi.ac.uk/pdbsum/7u9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7u9g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | |||
Rabies infection is nearly 100% lethal if untreated and kills more than 50,000 people annually, many of them children. Existing rabies vaccines target the rabies virus glycoprotein (RABV-G) but generate short-lived immune responses, likely because the protein is heterogeneous under physiological conditions. Here, we report the 3.39 A cryo-electron microscopy structure of trimeric, prefusion RABV-G complexed with RVA122, a potently neutralizing human antibody. RVA122 binds to a quaternary epitope at the top of RABV-G, bridging domains and stabilizing RABV-G protomers in a prefusion state. RABV-G trimerization involves side-to-side interactions between the central alpha helix and adjacent loops, rather than contacts between central helices, and interactions among the fusion loops at the glycoprotein base. These results provide a basis from which to develop improved rabies vaccines based on RABV-G stabilized in the prefusion conformation. | |||
Structure of the rabies virus glycoprotein trimer bound to a prefusion-specific neutralizing antibody.,Callaway HM, Zyla D, Larrous F, de Melo GD, Hastie KM, Avalos RD, Agarwal A, Corti D, Bourhy H, Saphire EO Sci Adv. 2022 Jun 17;8(24):eabp9151. doi: 10.1126/sciadv.abp9151. Epub 2022 Jun , 17. PMID:35714192<ref>PMID:35714192</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7u9g" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 12:14, 17 October 2024
Rabies virus glycoprotein pre-fusion trimer in complex with neutralizing antibody RVA122Rabies virus glycoprotein pre-fusion trimer in complex with neutralizing antibody RVA122
Structural highlights
Publication Abstract from PubMedRabies infection is nearly 100% lethal if untreated and kills more than 50,000 people annually, many of them children. Existing rabies vaccines target the rabies virus glycoprotein (RABV-G) but generate short-lived immune responses, likely because the protein is heterogeneous under physiological conditions. Here, we report the 3.39 A cryo-electron microscopy structure of trimeric, prefusion RABV-G complexed with RVA122, a potently neutralizing human antibody. RVA122 binds to a quaternary epitope at the top of RABV-G, bridging domains and stabilizing RABV-G protomers in a prefusion state. RABV-G trimerization involves side-to-side interactions between the central alpha helix and adjacent loops, rather than contacts between central helices, and interactions among the fusion loops at the glycoprotein base. These results provide a basis from which to develop improved rabies vaccines based on RABV-G stabilized in the prefusion conformation. Structure of the rabies virus glycoprotein trimer bound to a prefusion-specific neutralizing antibody.,Callaway HM, Zyla D, Larrous F, de Melo GD, Hastie KM, Avalos RD, Agarwal A, Corti D, Bourhy H, Saphire EO Sci Adv. 2022 Jun 17;8(24):eabp9151. doi: 10.1126/sciadv.abp9151. Epub 2022 Jun , 17. PMID:35714192[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||