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Figure 2.
Figure 2. Interface between the Skap-hom PH and DM Domains
(A) The PH domain is shown in red and the DM domain in blue
and green as in Figure 1C. Salt bridges are indicated by dashed
lines. Note the helical conformation of the β1-β2 loop
(residues Arg127–Phe135) and the insertion of PH domain
residues Phe132 and Leu133 into a hydrophobic pocket on the DM
domain.
(B) Stereo representation of the DM domain showing
the side chains of all residues, with salt bridges highlighted.
Representative charged residues are labeled.
(C) View of
one subunit of the DM domain showing the hydrophobic and charged
residues in the dimerization interface.
(D) Superposition
of the Skap-hom DM (green and blue) and the dimerization domain
of nuclear export protein Nep/Ns2 of influenza A (magenta)
(Akarsu et al., 2003), which shares a similar overall topology
but no clear sequence relationship.
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