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Figure 3.
Figure 3. Structural and Functional Relationship between the
IMD and BAR Domains
(A) Electrostatic surface
representation of the IMD dimer calculated with the program APBS
(Baker et al., 2001) and displayed with the program PyMOL
(http://www.pymol.org). Red and blue indicate negatively and
positively charged regions, respectively (red, −6 kTe^−1;
blue +6 kTe^−1). Note the positively charged and slightly
convex surface, which is thought to mediate the interactions
with membranes of the IMD (Suetsugu et al., 2006).
(B)
Similar electrostatic representation of the BAR domain of
amphiphysin (Peter et al., 2004). The orientation is the same as
in (A). Note that the shape of the positively charged membrane
binding surface of the BAR domain is concave.
(C)
Superimposition of the structures of the IMD of MIM (blue,
yellow) with that of the BAR domain of arfaptin complexed with
Rac (Tarricone et al., 2001) (gray). The orientation is the same
as in (A) and (B). The two folds have different curvatures, but
superimpose well in the middle section where the dimers overlap,
suggesting that this region may also mediate the binding of Rac
in MIM and IRSp53.
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