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Figure 5.
Figure 5. Crystal Structure of a D-Peptide Bound to the
gp41 Pocket(A) Ribbon representation of the overall structure of
the IQN17/D10-p1 complex. The GCN4-pI[Q]I′ part of the chimera
(dark blue) and the HIV-1 gp41 hydrophobic segment (gray) form a
continuous three-stranded coiled coil. Three D10-p1 inhibitors
(purple and green) bind solely to the hydrophobic pocket. The
six residues of the D-peptide that make direct contact with
IQN17 are shown in green (Gly-1, Ala-2, Trp-10, Trp-12, Leu-13,
and Ala-16). Figure drawn with Insight II 98.0 (Molecular
Simulations Inc.).(B) Stereo view of the IQN17/D10-p1 complex in
which IQN17 is represented as a molecular surface and D10-p1 is
represented with sticks. The color scheme is as in (A). The four
conserved residues of the EWXWL motif (Glu-9, Trp-10, Trp-12,
and Leu-13) are labeled. Figure drawn with Insight II 98.0
(Molecular Simulations Inc.).(C) Stereo view of a region of the
final 1.5 Å 2Fo-Fc map, contoured at 2.1σ, superimposed
on the final model. The view is approximately the same
orientation as in (B). Figure drawn with O ([26]).
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