5js9: Difference between revisions
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==Uncleaved prefusion optimized gp140 trimer with an engineered 8-residue HR1 turn bound to broadly neutralizing antibodies 8ANC195 and PGT128== | ==Uncleaved prefusion optimized gp140 trimer with an engineered 8-residue HR1 turn bound to broadly neutralizing antibodies 8ANC195 and PGT128== | ||
<StructureSection load='5js9' size='340' side='right' caption='[[5js9]], [[Resolution|resolution]] 6.92Å' scene=''> | <StructureSection load='5js9' size='340' side='right'caption='[[5js9]], [[Resolution|resolution]] 6.92Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5js9]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/9hiv1 9hiv1] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JS9 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5js9]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/9hiv1 9hiv1] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JS9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JS9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jsa|5jsa]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jsa|5jsa]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5js9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5js9 OCA], [http://pdbe.org/5js9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5js9 RCSB], [http://www.ebi.ac.uk/pdbsum/5js9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5js9 ProSAT]</span></td></tr> | ||
</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]] | ||
*[[Gp120|Gp120]] | *[[Gp120 3D structures|Gp120 3D structures]] | ||
*[[Gp41|Gp41]] | *[[Gp41 3D Structures|Gp41 3D Structures]] | ||
*[[3D structures of human antibody|3D structures of human antibody]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Kong, L]] | [[Category: Kong, L]] | ||
[[Category: Wilson, I A]] | [[Category: Wilson, I A]] | ||
Revision as of 14:36, 17 June 2020
Uncleaved prefusion optimized gp140 trimer with an engineered 8-residue HR1 turn bound to broadly neutralizing antibodies 8ANC195 and PGT128Uncleaved prefusion optimized gp140 trimer with an engineered 8-residue HR1 turn bound to broadly neutralizing antibodies 8ANC195 and PGT128
Structural highlights
Publication Abstract from PubMedThe trimeric HIV-1 envelope glycoprotein (Env) is critical for host immune recognition and neutralization. Despite advances in trimer design, the roots of Env trimer metastability remain elusive. Here we investigate the contribution of two Env regions to metastability. First, we computationally redesign a largely disordered bend in heptad region 1 (HR1) of SOSIP trimers that connects the long, central HR1 helix to the fusion peptide, substantially improving the yield of soluble, well-folded trimers. Structural and antigenic analyses of two distinct HR1 redesigns confirm that redesigned Env closely mimics the native, prefusion trimer with a more stable gp41. Next, we replace the cleavage site between gp120 and gp41 with various linkers in the context of an HR1 redesign. Electron microscopy reveals a potential fusion intermediate state for uncleaved trimers containing short but not long linkers. Together, these results outline a general approach for stabilization of Env trimers from diverse HIV-1 strains. Uncleaved prefusion-optimized gp140 trimers derived from analysis of HIV-1 envelope metastability.,Kong L, He L, de Val N, Vora N, Morris CD, Azadnia P, Sok D, Zhou B, Burton DR, Ward AB, Wilson IA, Zhu J Nat Commun. 2016 Jun 28;7:12040. doi: 10.1038/ncomms12040. PMID:27349805[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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