Article
A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: implication for viral fusion.
Journal of virology - 1 Jun 1995
Chen C H, Matthews T J, McDanal C B, Bolognesi D P, Greenberg M L
Abstract excerpt
We have previously reported that synthetic peptides representing the leucine zipper domain (DP107) and a second putative helical domain (DP178) of human immunodeficiency virus type 1 (HIV-1) gp41 exhibit potent anti-HIV activity. In this study we have used soluble recombinant forms of gp41 to pro...
Topics
- Antiviral Agents
- Base Sequence
- Cell Line
- DNA Primers
- Epitopes
- HIV Envelope Protein gp41
- HIV-1
- Humans
- Leucine Zippers
- Membrane Fusion
- Molecular Sequence Data
- Mutation
- Recombinant Fusion Proteins
- Structure-Activity Relationship