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PDBsum entry 1lcx
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Viral protein
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PDB id
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1lcx
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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A monomeric 3(10)-Helix is formed in water by a 13-Residue peptide representing the neutralizing determinant of HIV-1 on gp41.
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Authors
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Z.Biron,
S.Khare,
A.O.Samson,
Y.Hayek,
F.Naider,
J.Anglister.
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Ref.
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Biochemistry, 2002,
41,
12687-12696.
[DOI no: ]
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PubMed id
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Abstract
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The peptide gp41(659-671) (ELLELDKWASLWN) comprises the entire epitope for one
of the three known antibodies capable of neutralizing a broad spectrum of
primary HIV-1 isolates and is the only such epitope that is sequential. Here we
present the NMR structure of gp41(659-671) in water. This peptide forms a
monomeric 3(10)-helix stabilized by i,i+3 side chain-side chain interactions
favored by its primary sequence. In this conformation the peptide presents an
exposed surface, which is mostly hydrophobic and consists of conserved HIV-1
residues. The presence of the 3(10)-helix is confirmed by its characteristic CD
pattern. Studies of the 3(10)-helix have been hampered by the absence of a model
peptide adopting this conformation. gp41(659-671) can serve as such a model to
investigate the spectral characteristics of the 3(10)-helix, the factors that
influence its stability, and the propensity of different amino acids to form a
3(10)-helix. The observation that the 3(10)-helical conformation is highly
populated in the peptide gp41(659-671) indicates that the corresponding segment
in the cognate protein is an autonomous folding unit. As such, it is very likely
that the helical conformation is maintained in gp41 throughout the different
tertiary structures of the envelope protein that form during the process of
viral fusion. However, the exposure of the gp41(659-671) segment may vary,
leading to changes in the reactivity of anti-gp41 antibodies in the different
stages of viral fusion. Since gp41(659-671) is an autonomous folding unit,
peptide immunogens consisting of the complete gp41(659-671) sequence are likely
to induce antibodies highly cross-reactive with HIV-1.
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