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Figure 2.
Figure 2. Views of Key Residues of the Bound IQ Peptide
with CaM Surfaces
The residues of the peptide are in
magenta, electron density is blue. Protein surface
representations are: dark blue, +; red, -; cyan, neutral or
nonpolar; and yellow, sulfur of methionine residues.
(A)
Cutaway view of the complex. CaM domains are labeled, along with
selected peptide residues. The N-terminal pocket of Ca^2+-CaM
(containing F1666 of the peptide) is to the left of center. Some
residues at the C-terminal end of the peptide extend above the
plane of the figure and are not shown.
(B) The N-terminal
hydrophobic cluster of the IQ peptide. F1666 (center background)
occupies the N-terminal hydrophobic pocket of Ca^2+CaM. The
surface is the CaM binding channel, with the N domain of
Ca^2+-CaM to the left and the C domain to the right. F1670,
Y1667, and L1671 are grouped near a nonpolar surface created by
the Ca^2+-CaM linker (lower foreground). This hydrophobic
surface is created by M71, M72, M76, and the hydrophobic portion
of the K75-E84 salt link.
(C) The C-terminal hydrophobic
cluster of the IQ peptide. The surface is the C-terminal
hydrophobic pocket of Ca^2+-CaM.
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