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Figure 3.
Figure 3. Superposition of (a) unliganded RT and RT–DNA–Fab
complex and (b) unliganded RT and RT–α-APA
(α-anilinophenylacetamide) complex based on 89 Cα atoms in the
p66 palm subdomain, including the β6–β10–β9 region. The
unliganded RT is shown in red, RT–α-APA in blue, and
RT–DNA–Fab in green. A comparison of the two superpositions
reveals that NNRTI binding appears to be accompanied by a
long-range distortion that is coupled with a hinge motion
(indicated by curved arrows) between the β6–β10–β9 and
β12–β13–β14 sheets at the p66 palm subdomain (within the
circle). The different positions of the thumb in different HIV-1
RT structures supports the idea that this subdomain could play
a role during polymerization. Figure 3. Superposition of (a)
unliganded RT and RT–DNA–Fab complex and (b) unliganded RT
and RT–α-APA (α-anilinophenylacetamide) complex based on 89
Cα atoms in the p66 palm subdomain, including the
β6–β10–β9 region. The unliganded RT is shown in red,
RT–α-APA in blue, and RT–DNA–Fab in green. A comparison
of the two superpositions reveals that NNRTI binding appears to
be accompanied by a long-range distortion that is coupled with a
hinge motion (indicated by curved arrows) between the
β6–β10–β9 and β12–β13–β14 sheets at the p66 palm
subdomain (within the circle). The different positions of the
thumb in different HIV-1 RT structures supports the idea that
this subdomain could play a role during polymerization.
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