Article
Unique functional properties of conserved arginine residues in the lentivirus lytic peptide domains of the C-terminal tail of HIV-1 gp41.
The Journal of biological chemistry - 14 Mar 2014
Kuhlmann Anne-Sophie, Steckbeck Jonathan D, Sturgeon Timothy J, Craigo Jodi K, Montelaro Ronald C
Abstract excerpt
A previous study from our laboratory reported a preferential conservation of arginine relative to lysine in the C-terminal tail (CTT) of HIV-1 envelope (Env). Despite substantial overall sequence variation in the CTT, specific arginines are highly conserved in the lentivirus lytic peptide (LLP) motifs and are scarcely substituted by lysines, in contrast to gp120 and the ectodomain of gp41. However, to date, no...
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