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Figure 2.
Figure 2. Overall Structure of the Kinase Domain of
Rho-Kinase and Comparison with PKA
(A) Ribbon diagram of
Rho-kinase (molecules A). The kinase domain with the C-terminal
extension is shown in cyan (N-terminal lobe), blue (C-terminal
lobe), and red (C-terminal extension containing the hydrophobic
motif). The N-terminal extension forming the CHB domain is
omitted for clarity. All secondary structure elements are
labeled. The bound fasudil is shown as a stick model. Five
catalytically important residues (Lys121, Glu140, Asp214,
Asn219, and Asp232) in addition to the potential phosphorylation
site in the activation loop (Thr249) are shown. The functional
motifs are shown with the same color scheme as in Figure 1A;
magenta, P loop; orange, C loop; yellow, A loop. Dotted
connections between the N-terminal lobe and the C-terminal
extension are for residues omitted in model building due to poor
electron density (see text).
(B) Ribbon diagram of PKA (PDB
code: 1CDK). The bound ATP analog (AMPPNP) is shown as a stick
model. Five catalytically important residues (Lys72, Glu91,
Asp166, Asn171, and Asp184) and the phosphorylated threonine
(pThr197) in the activation loop are shown. The functionally
significant motifs are shown with the same color scheme as in
(A). The PKI peptide is not shown for clarity.
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