6tou: Difference between revisions
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<StructureSection load='6tou' size='340' side='right'caption='[[6tou]], [[Resolution|resolution]] 2.59Å' scene=''> | <StructureSection load='6tou' size='340' side='right'caption='[[6tou]], [[Resolution|resolution]] 2.59Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6tou]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TOU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6TOU FirstGlance]. <br> | <table><tr><td colspan='2'>[[6tou]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Rabies_lyssavirus Rabies lyssavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TOU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6TOU FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">scFv ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6tou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tou OCA], [http://pdbe.org/6tou PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tou RCSB], [http://www.ebi.ac.uk/pdbsum/6tou PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tou 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=6tou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tou OCA], [http://pdbe.org/6tou PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tou RCSB], [http://www.ebi.ac.uk/pdbsum/6tou PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tou ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Rabies virus (RABV) causes fatal encephalitis in more than 59,000 people yearly. Upon the bite of an infected animal, the development of clinical disease can be prevented with post-exposure prophylaxis (PEP), which includes the administration of Rabies immunoglobulin (RIG). However, the high cost and limited availability of serum-derived RIG severely hamper its wide use in resource-limited countries. A safe low-cost alternative is provided by using broadly neutralizing monoclonal antibodies (bnAbs). Here we report the X-ray structure of one of the most potent and most broadly reactive human bnAbs, RVC20, in complex with its target domain III of the RABV glycoprotein (G). The structure reveals that the RVC20 binding determinants reside in a highly conserved surface of G, rationalizing its broad reactivity. We further show that RVC20 blocks the acid-induced conformational change required for membrane fusion. Our results may guide the future development of direct antiviral small molecules for Rabies treatment. | |||
Structure of the prefusion-locking broadly neutralizing antibody RVC20 bound to the rabies virus glycoprotein.,Hellert J, Buchrieser J, Larrous F, Minola A, de Melo GD, Soriaga L, England P, Haouz A, Telenti A, Schwartz O, Corti D, Bourhy H, Rey FA Nat Commun. 2020 Jan 30;11(1):596. doi: 10.1038/s41467-020-14398-7. PMID:32001700<ref>PMID:32001700</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6tou" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Rabies lyssavirus]] | |||
[[Category: Hellert, J]] | [[Category: Hellert, J]] | ||
[[Category: Rey, F A]] | [[Category: Rey, F A]] | ||
Revision as of 10:38, 19 February 2020
Rabies virus glycoprotein PH domain in complex with the scFv fragment of broadly neutralizing human antibody RVC20Rabies virus glycoprotein PH domain in complex with the scFv fragment of broadly neutralizing human antibody RVC20
Structural highlights
Publication Abstract from PubMedRabies virus (RABV) causes fatal encephalitis in more than 59,000 people yearly. Upon the bite of an infected animal, the development of clinical disease can be prevented with post-exposure prophylaxis (PEP), which includes the administration of Rabies immunoglobulin (RIG). However, the high cost and limited availability of serum-derived RIG severely hamper its wide use in resource-limited countries. A safe low-cost alternative is provided by using broadly neutralizing monoclonal antibodies (bnAbs). Here we report the X-ray structure of one of the most potent and most broadly reactive human bnAbs, RVC20, in complex with its target domain III of the RABV glycoprotein (G). The structure reveals that the RVC20 binding determinants reside in a highly conserved surface of G, rationalizing its broad reactivity. We further show that RVC20 blocks the acid-induced conformational change required for membrane fusion. Our results may guide the future development of direct antiviral small molecules for Rabies treatment. Structure of the prefusion-locking broadly neutralizing antibody RVC20 bound to the rabies virus glycoprotein.,Hellert J, Buchrieser J, Larrous F, Minola A, de Melo GD, Soriaga L, England P, Haouz A, Telenti A, Schwartz O, Corti D, Bourhy H, Rey FA Nat Commun. 2020 Jan 30;11(1):596. doi: 10.1038/s41467-020-14398-7. PMID:32001700[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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