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Figure 2.
Figure 2. Comparison of the complex with other CaM -target
peptide complexes. a, Ribbon representation of the MARCKS
peptide -CaM complex compared with other globular-type CaM
-target peptide complexes: MLCK (PDB entry 1CDL), CaMKII (1CDM)
and CaMKK (1IQ5). The N- and C-lobe of CaM are shown in green
and blue, respectively. The target peptides are shown in red.
Ca^2+ ions are shown as black spheres. The figures were produced
using MolScript40 and Raster3D^41. The target peptides are shown
in red. The key hydrophobic residues of target peptides anchored
to either of the N- or C-lobes of CaM are shown in
ball-and-stick representations and labeled. Electrostatic
surface representations of CaM N-lobe with b, MARCKS peptide and
c, MLCK peptide^8 and C-lobe with d, edema factor (EF)19. In
(d), only part of helix H of EF (residues 521 -537), which
interacts with Ca^2+-bound C-lobe of CaM, was shown. The
hydrophobic pocket of CaM observed in (c,d) is flattened in (b)
and is not involved in the interaction with MARCKS peptide.
Hydrophobic residues of MARCKS peptide interacting with CaM
N-lobe, Leu159 and Phe162, are located on different hydrophobic
surfaces of CaM. The figures were generated using GRASP42. e,
Superimposition of CaM N-lobe of the MARCKS peptide -Ca^2+-CaM
(yellow) onto those of the MLCK peptide -Ca^2+-CaM8 (green). The
MARCKS and MLCK peptides are shown in red and orange,
respectively.
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