Figure 1 - full size



	Figure 1 - full size

Figure 1.
FIGURE 1. Overall structure of the ROCK/Y-27632 complex. A, the ROCK protein dimer is drawn with -sheets as arrows and -helices as cylinders. One monomer is drawn in gray, and the others are colored by protein region. The N-terminal dimerization domain is shown in red. The N-terminal kinase domain (dark blue) is shown with the glycine-rich loop drawn in green. The hinge connecting the two domains is colored orange. The C-terminal kinase domain is shown in light blue with the activation loop in purple and the kinase tail in yellow. Y-27632 is shown in the active site near the glycine-rich loop and the hinge. B, a surface representation of the dimer is shown where both monomers are colored by region. Y-27632 is shown in the active site as spheres. A model of the substrate peptide is shown as a pink cylinder and strand, based upon a superposition of the ROCK structure and the PKA/ATP/peptide complex (Protein Data Bank code 1ATP [PDB] ). C and D, an expanded view of the dimerization domain is shown in two orientations, differing by a 90° rotation. All of the structure figures were made with PYMOL (58).