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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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References listed in PDB file
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Key reference
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Title
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Capturing the inherent structural dynamics of the HIV-1 envelope glycoprotein fusion peptide.
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Authors
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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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Ref.
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Nat Commun, 2019,
10,
763.
[DOI no: ]
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PubMed id
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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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