5cck: Difference between revisions
New page: '''Unreleased structure''' The entry 5cck is ON HOLD Authors: Lee, J.H., Ward, A.B., Wilson, I.A. Description: Crystal structure of Human anti-HIV-1 broadly neutralizing antibody 3BC31... |
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==Crystal structure of Human anti-HIV-1 broadly neutralizing antibody 3BC315 Fab== | |||
<StructureSection load='5cck' size='340' side='right'caption='[[5cck]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5cck]] 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=5CCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CCK 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]] 1.95Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</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=5cck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cck OCA], [https://pdbe.org/5cck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cck RCSB], [https://www.ebi.ac.uk/pdbsum/5cck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cck ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The recent identification of three broadly neutralizing antibodies (bnAbs) against gp120-gp41 interface epitopes has expanded the targetable surface on the HIV-1 envelope glycoprotein (Env) trimer. By using biochemical, biophysical and computational methods, we map the previously unknown trimer epitopes of two related antibodies, 3BC315 and 3BC176. A cryo-EM reconstruction of a soluble Env trimer bound to 3BC315 Fab at 9.3 A resolution reveals that the antibody binds between two gp41 protomers, and neutralizes the virus by accelerating trimer decay. In contrast, bnAb 35O22 binding to a partially overlapping quaternary epitope at the gp120-gp41 interface does not induce decay. A conserved gp41-proximal glycan at N88 was also shown to play a role in the binding kinetics of 3BC176 and 3BC315. Finally, our data suggest that the dynamic structure of the Env trimer influences exposure of bnAb epitopes. | |||
Antibodies to a conformational epitope on gp41 neutralize HIV-1 by destabilizing the Env spike.,Lee JH, Leaman DP, Kim AS, Torrents de la Pena A, Sliepen K, Yasmeen A, Derking R, Ramos A, de Taeye SW, Ozorowski G, Klein F, Burton DR, Nussenzweig MC, Poignard P, Moore JP, Klasse PJ, Sanders RW, Zwick MB, Wilson IA, Ward AB Nat Commun. 2015 Sep 25;6:8167. doi: 10.1038/ncomms9167. PMID:26404402<ref>PMID:26404402</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5cck" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Wilson | ==See Also== | ||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[Sandbox 20009|Sandbox 20009]] | |||
*[[3D structures of human antibody|3D structures of human antibody]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Lee JH]] | |||
[[Category: Ward AB]] | |||
[[Category: Wilson IA]] | |||
Latest revision as of 10:02, 17 October 2024
Crystal structure of Human anti-HIV-1 broadly neutralizing antibody 3BC315 FabCrystal structure of Human anti-HIV-1 broadly neutralizing antibody 3BC315 Fab
Structural highlights
Publication Abstract from PubMedThe recent identification of three broadly neutralizing antibodies (bnAbs) against gp120-gp41 interface epitopes has expanded the targetable surface on the HIV-1 envelope glycoprotein (Env) trimer. By using biochemical, biophysical and computational methods, we map the previously unknown trimer epitopes of two related antibodies, 3BC315 and 3BC176. A cryo-EM reconstruction of a soluble Env trimer bound to 3BC315 Fab at 9.3 A resolution reveals that the antibody binds between two gp41 protomers, and neutralizes the virus by accelerating trimer decay. In contrast, bnAb 35O22 binding to a partially overlapping quaternary epitope at the gp120-gp41 interface does not induce decay. A conserved gp41-proximal glycan at N88 was also shown to play a role in the binding kinetics of 3BC176 and 3BC315. Finally, our data suggest that the dynamic structure of the Env trimer influences exposure of bnAb epitopes. Antibodies to a conformational epitope on gp41 neutralize HIV-1 by destabilizing the Env spike.,Lee JH, Leaman DP, Kim AS, Torrents de la Pena A, Sliepen K, Yasmeen A, Derking R, Ramos A, de Taeye SW, Ozorowski G, Klein F, Burton DR, Nussenzweig MC, Poignard P, Moore JP, Klasse PJ, Sanders RW, Zwick MB, Wilson IA, Ward AB Nat Commun. 2015 Sep 25;6:8167. doi: 10.1038/ncomms9167. PMID:26404402[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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