4ut7: Difference between revisions
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<StructureSection load='4ut7' size='340' side='right'caption='[[4ut7]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='4ut7' size='340' side='right'caption='[[4ut7]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ut7]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ut7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UT7 FirstGlance]. <br> | ||
</td></tr> | </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=4ut7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ut7 OCA], [https://pdbe.org/4ut7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ut7 RCSB], [https://www.ebi.ac.uk/pdbsum/4ut7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ut7 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[Antibody 3D structures|Antibody 3D structures]] | *[[Antibody 3D structures|Antibody 3D structures]] | ||
*[[3D structures of human antibody|3D structures of human antibody]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Barba-Spaeth | [[Category: Barba-Spaeth G]] | ||
[[Category: Duquerroy | [[Category: Duquerroy S]] | ||
[[Category: Guardado-Calvo | [[Category: Guardado-Calvo P]] | ||
[[Category: Rey | [[Category: Rey FA]] | ||
[[Category: Rouvinski | [[Category: Rouvinski A]] | ||
[[Category: Vaney | [[Category: Vaney MC]] | ||
Revision as of 10:37, 29 March 2023
CRYSTAL STRUCTURE OF THE SCFV FRAGMENT OF THE BROADLY NEUTRALIZING HUMAN ANTIBODY EDE2 A11CRYSTAL STRUCTURE OF THE SCFV FRAGMENT OF THE BROADLY NEUTRALIZING HUMAN ANTIBODY EDE2 A11
Structural highlights
Publication Abstract from PubMedDengue disease is caused by four different flavivirus serotypes, which infect 390 million people yearly with 25% symptomatic cases and for which no licensed vaccine is available. Recent phase III vaccine trials showed partial protection, and in particular no protection for dengue virus serotype 2 (refs 3, 4). Structural studies so far have characterized only epitopes recognized by serotype-specific human antibodies. We recently isolated human antibodies potently neutralizing all four dengue virus serotypes. Here we describe the X-ray structures of four of these broadly neutralizing antibodies in complex with the envelope glycoprotein E from dengue virus serotype 2, revealing that the recognition determinants are at a serotype-invariant site at the E-dimer interface, including the exposed main chain of the E fusion loop and the two conserved glycan chains. This 'E-dimer-dependent epitope' is also the binding site for the viral glycoprotein prM during virus maturation in the secretory pathway of the infected cell, explaining its conservation across serotypes and highlighting an Achilles' heel of the virus with respect to antibody neutralization. These findings will be instrumental for devising novel immunogens to protect simultaneously against all four serotypes of dengue virus. Recognition determinants of broadly neutralizing human antibodies against dengue viruses.,Rouvinski A, Guardado-Calvo P, Barba-Spaeth G, Duquerroy S, Vaney MC, Kikuti CM, Navarro Sanchez ME, Dejnirattisai W, Wongwiwat W, Haouz A, Girard-Blanc C, Petres S, Shepard WE, Despres P, Arenzana-Seisdedos F, Dussart P, Mongkolsapaya J, Screaton GR, Rey FA Nature. 2015 Jan 12. doi: 10.1038/nature14130. PMID:25581790[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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