Download MendeleyThe complete Consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solution.
Vranken, W.F., Budesinsky, M., Fant, F., Boulez, K., Borremans, F.A.(1995) FEBS Lett 374: 117-121
- PubMed: 7589496
- DOI: https://doi.org/10.1016/0014-5793(95)01086-t
- Primary Citation of Related Structures:
1CE4 - PubMed Abstract:
The disulfide bridge closed cyclic peptide corresponding to the whole Consensus V3 loop of the envelope protein gp120 of HIV-1 was examined by proton 2D-NMR spectroscopy in water and in a 20% trifluoroethanol/water solution. In water, NOE data support a beta-turn conformation for the central conservative GPGR region and point towards partial formation of a helix in the C-terminal part. Upon addition of trifluoroethanol, a C-terminal helix is formed. This is evidenced by NOE data, alpha-proton chemical shift changes and changes in the JN alpha vicinal coupling constants. The C-terminal helix is amphipathic and also occurs in other examined strains. It could therefore be an important feature for the functioning of the V3 loop.
Organizational Affiliation:
Department of Organic Chemistry, University of Gent, Belgium.
