Abstract: Further studies, using recombinant
RTs obtained by site-directed mutagenesis, revealed that
M41L,
A62V and in a lesser extent
K70R, were the key mutations that together with
T69S,
T215Y and the dipeptide insertion conferred high levels of ATP-dependent phosphorolytic activity on AZT and d4T-terminated primers.
Abstract: Structural analysis of the location of the implicated amino acid substitutions revealed a coordinated effect of
M41L and
A62V on the positioning of the beta3-beta4 hairpin loop, which plays a key role in the resistance mechanism.