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PDBsum entry 6mdt
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Viral protein
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PDB id
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6mdt
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Contents |
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136 a.a.
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455 a.a.
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240 a.a.
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213 a.a.
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231 a.a.
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211 a.a.
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PDB id:
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| Name: |
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Viral protein
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Title:
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Crystal structure of the b41 sosip.664 env trimer with pgt124 and 35o22 fabs, in p63 space group
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Structure:
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Transmembrane protein gp41. Chain: b. Fragment: residues 516-668. Synonym: tm. Engineered: yes. Surface protein gp120. Chain: g. Fragment: residues 30-511. Synonym: su, glycoprotein 120, gp120.
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Source:
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Human immunodeficiency virus 1. Organism_taxid: 11676. Gene: env. Expressed in: homo sapiens. Expression_system_taxid: 9606. Homo sapiens. Human. Organism_taxid: 9606. Expression_system_taxid: 9606
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Resolution:
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3.82Å
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R-factor:
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0.295
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R-free:
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0.311
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Authors:
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S.Kumar,A.Sarkar,I.A.Wilson
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Key ref:
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S.Kumar
et al.
(2019).
Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide.
Nat Commun,
10,
763.
PubMed id:
DOI:
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Date:
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05-Sep-18
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Release date:
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27-Feb-19
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PROCHECK
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Headers
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References
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B3UES2
(B3UES2_9HIV1) -
Envelope glycoprotein gp160 from Human immunodeficiency virus type 1
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Seq:
Struc:
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860 a.a.
136 a.a.*
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B3UF58
(B3UF58_9HIV1) -
Envelope glycoprotein gp160 from Human immunodeficiency virus type 1
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Seq:
Struc:
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860 a.a.
455 a.a.*
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No UniProt id for this chain
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No UniProt id for this chain
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DOI no:
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Nat Commun
10:763
(2019)
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PubMed id:
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Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide.
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S.Kumar,
A.Sarkar,
P.Pugach,
R.W.Sanders,
J.P.Moore,
A.B.Ward,
I.A.Wilson.
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ABSTRACT
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The N-terminal fusion peptide (FP) of the human immunodeficiency virus (HIV)-1
envelope glycoprotein (Env) gp41 subunit plays a critical role in cell entry.
However, capturing the structural flexibility in the unbound FP is challenging
in the native Env trimer. Here, FP conformational isomerism is observed in two
crystal structures of a soluble clade B transmitted/founder virus B41 SOSIP.664
Env with broadly neutralizing antibodies (bNAbs) PGT124 and 35O22 to aid in
crystallization and that are not specific for binding to the FP. Large
rearrangements in the FP and fusion peptide proximal region occur around M530,
which remains anchored in the tryptophan clasp (gp41 W623, W628, W631) in the
B41 Env prefusion state. Further, we redesigned the FP at position 518 to
reinstate the bNAb VRC34.01 epitope. These findings provide further structural
evidence for the dynamic nature of the FP and how a bNAb epitope can be restored
during vaccine design.
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