Figure 10.

Location of photolabeled residues in the modeled PKCδ C1A structure. Modeled structure of PKCδ C1A showing the positions of the photolabeled residues listed in Table 2. Tyr-29 and Lys-40 are in contact forming one site, whereas Glu-2 is more distant. The model is based on the published crystal structure of PKCδ C1B (Zhang et al. 1995), with all residues mutated to their equivalents in PKCδ C1A. The backbone and side-chain carbon atoms are colored light blue for residues that are conserved and plum for residues that are not conserved between C1A and C1B. The side-chain carbons of Tyr-29, Glu-2, and Lys-40 are colored gold, cyan, and orange, respectively. The zinc atoms, which each coordinate three conserved cysteines and one conserved histidine, are shown in dark blue. Molecular graphics images were produced by using the UCSF Chimera package from the Computer Graphics Laboratory, University of California, San Francisco (supported by NIH P41 RR-01081) (Pettersen et al. 2004).