Figure 7.
Figure 7 Comparison of the interactions of CaM with its
effectors. (A) Representative structures of CaM in complex with
its effectors. N-CaM is colored orange and C-CaM red. The
segment from CaM effectors is colored purple and the second
molecule of the dimer of CaM effectors is cyan. The protein data
bank accession numbers, 1CDL, 1IWQ, 1L7Z, 1NWD, 1G4Y, and 1YRT,
for CaM in complex with MLCK, MARCKS, CAP-23/NAP-22, GAD,
calcium-activated small-conductance potassium channel (SK2), and
CyaA, respectively. (B) Comparison of the interaction of C-CaM
with the H helix of CyaA -ACD and the amphipathic -helix
of MLCK. The helices of CaM are colored red and the atoms,
carbon, oxygen, nitrogen, and sulfur, are gray, red, blue, and
yellow, respectively. (C) Interaction of CaM with its effectors.
Sequence and secondary structure of the C-terminal of CaM are
shown on the top. The Ca^2+-binding sites are marked and
Ca^2+-binding residues are colored red. Boxes beneath the
sequence of C-CaM indicate the contact area of each residue in
the various structures, using the same coloring scheme as in
Figure 4C. The Protein Data Bank codes for the structures are
1CKK, 1CDM, 1IQ5, and 1K90 for CaM in complex with CaM kinase I
(CaMKI), CaM kinase II (CaMKII), CaM kinase kinase (CaMKK), and
EF, respectively. Helix designations above the CaM sequence are
based on the 1CLL CaM structure.
-helix
of MLCK. The helices of CaM are colored red and the atoms,
carbon, oxygen, nitrogen, and sulfur, are gray, red, blue, and
yellow, respectively. (C) Interaction of CaM with its effectors.
Sequence and secondary structure of the C-terminal of CaM are
shown on the top. The Ca^2+-binding sites are marked and
Ca^2+-binding residues are colored red. Boxes beneath the
sequence of C-CaM indicate the contact area of each residue in
the various structures, using the same coloring scheme as in
Figure 4C. The Protein Data Bank codes for the structures are
1CKK, 1CDM, 1IQ5, and 1K90 for CaM in complex with CaM kinase I
(CaMKI), CaM kinase II (CaMKII), CaM kinase kinase (CaMKK), and
EF, respectively. Helix designations above the CaM sequence are
based on the 1CLL CaM structure.