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Figure 6.
Figure 6. (a) The docking of the PKCa-C2-Ca^2+-DCPS ternary
complex onto a model membrane and (b) the superimposition of the
structures from the PKCs C2 domains a and e suggest (c) a
docking mechanism for PKCe-C2. In this model only loop 3 appears
to penetrate into the lipid bilayer, though loop 1 would also be
in close contact with the membrane. In the model bulky
side-chains of Trp23, Ile89 and Tyr91 (explicitly depicted)
could reach the inner membrane while conserved basic residues
(particularly Arg26, Arg32, Arg50 and probably also His85) would
interact with the phospholipid charged heads (c). The
coordination of the Mg2+ might also facilitate the interaction
with the membrane (see the text). In this model the carboxy end
of the C2 domain, to be continued by the pseudo-substrate and
the C1 domain in the intact PKC, appears situated apart from the
membrane.
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