Figure 2.
(a) The CTD superimposed on active PKA (chain A from PDB
1CDK) illustrates the different positions of the D-helix.
Boxed region corresponds to boxed region in c. The ligand
(inhibitory peptide, purple ribbon) and an ATP analog (AMP-PNP;
blue van der Waals surface representation) bound to PKA are
included. (b) The CTD RSK2 superimposed on the autoinhibited
Ca^2+/calmodulin-dependent protein kinase I (PDB 1A06). (c) A
comparison of the active sites of CTD and PKA. Selected RSK2 CTD
residues are shown. Only residue Glu127 (analogous to Glu500 in
the CTD structure), which differs in the two structures, is
shown for PKA. The ATP analog and Mg^2+ ions (balls) are shown
in blue.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2008,
15,
112-113)
copyright 2008.
D-helix.
Boxed region corresponds to boxed region in c. The ligand
(inhibitory peptide, purple ribbon) and an ATP analog (AMP-PNP;
blue van der Waals surface representation) bound to PKA are
included. (b) The CTD RSK2 superimposed on the autoinhibited
Ca^2+/calmodulin-dependent protein kinase I (PDB 1A06). (c) A
comparison of the active sites of CTD and PKA. Selected RSK2 CTD
residues are shown. Only residue Glu127 (analogous to Glu500 in
the CTD structure), which differs in the two structures, is
shown for PKA. The ATP analog and Mg^2+ ions (balls) are shown
in blue.