1996
DOI: 10.1135/cccc19960742
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Conformational Features of a Synthetic Cyclic Peptide Corresponding to the Complete V3 Loop of the ELI HIV-1 Strain in Water

Abstract: The disulfide bridge closed cyclic peptide corresponding to the whole V3 loop of the envelope protein gp120 of the ELI HIV-1 strain was synthesized and examined by proton 2D NMR spectroscopy in water. Although the peptide is mainly conformationally flexible, a turn appears to be present at an N-terminal glycosylation site, while in the C-terminal half of the peptide the data point toward nascent helical structures. Similar conformational preferences in aqueous solution were observed in other V3 loop peptides, … Show more

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Cited by 4 publications
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“…If they can still adopt the conformation preferred by M‐tropic V3 loops despite having a higher positive charge, they could possess the putative features of both M‐ and T‐tropic strains. The structural studies on V3 loops from dual‐tropic and T‐tropic strains confirm this: some have a tendency to form a C‐terminal helix (MN [33,35] or RF [36,39]), but this is not a necessary requirement (IIIB [40] or ELI [38]). The ambiguous character of the HIV‐1 strains toward tropism might thus be based on their ability to form a C‐terminal amphipathic helix, which is in turn directed by the number and location of basic amino acid residues.…”
Section: Discussionmentioning
confidence: 92%
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“…If they can still adopt the conformation preferred by M‐tropic V3 loops despite having a higher positive charge, they could possess the putative features of both M‐ and T‐tropic strains. The structural studies on V3 loops from dual‐tropic and T‐tropic strains confirm this: some have a tendency to form a C‐terminal helix (MN [33,35] or RF [36,39]), but this is not a necessary requirement (IIIB [40] or ELI [38]). The ambiguous character of the HIV‐1 strains toward tropism might thus be based on their ability to form a C‐terminal amphipathic helix, which is in turn directed by the number and location of basic amino acid residues.…”
Section: Discussionmentioning
confidence: 92%
“…Despite its importance, relatively little is known about the conformation of the V3 loop. Free V3 loop peptides in aqueous solution are highly flexible, with some tendency towards helical conformations in their C‐terminal region [33–42]. The central residues of V3 loop peptides in complex with anti‐(gp120 V3 loop) Ig adopt a short β hairpin with a type II turn for the central GPGR region [43–46].…”
mentioning
confidence: 99%