Figure 2.
Figure 2 Superposition of the crystal structures of wild-type
HIV-1 protease complexed with (I) (blue) and (II) (green). The
80s loop, comprised of residues 79-83, and the flap residues
47-54 of the two monomers are depicted. The inhibitor structures
are represented as ball-and-stick models. (a) The P1-P3
(benzofuran) of (II) is sandwiched between the 80s loop and the
flap. Pro81 is pulled away by 2.0 Å in order to accommodate the
P1-P3 group. (b) The 2|F[o]| - |F[c]| map contoured at 1.0 represents
the electron density for the 80s loop in the complex of
wild-type protease with (II). The map was computed using phases
from the initial protein model without any inhibitor (blue)
which had been optimized by rigid-body refinement. The final
refined model of the 80s loop and the inhibitor (II) are
depicted in green. (c) The P1-P3 (pyridyl group in blue) of (I)
interacts with Arg8 and is exposed to solvent. In contrast, the
P1-P3 (benzofuran group in green) of (II) is sandwiched between
the 80s loop and the flap and does not interact with Arg8.
Instead, Arg8 interacts with the water molecules, represented as
colored dots.
The above figure is reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2000,
56,
381-388)
copyright 2000.
represents
the electron density for the 80s loop in the complex of
wild-type protease with (II). The map was computed using phases
from the initial protein model without any inhibitor (blue)
which had been optimized by rigid-body refinement. The final
refined model of the 80s loop and the inhibitor (II) are
depicted in green. (c) The P1-P3 (pyridyl group in blue) of (I)
interacts with Arg8 and is exposed to solvent. In contrast, the
P1-P3 (benzofuran group in green) of (II) is sandwiched between
the 80s loop and the flap and does not interact with Arg8.
Instead, Arg8 interacts with the water molecules, represented as
colored dots.