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. 2017 Feb 23;8:6. doi: 10.1038/s41467-016-0015-8

Fig. 2.

Fig. 2

Representative snapshots of PKCδ C1b–bryostatin–membrane complex. Green, blue, and red surfaces correspond to hydrophobic, basic, and acidic residues, respectively. In the more deeply embedded structure a, many hydrophobic residues are able to reside in the hydrocarbon region of the membrane, while the vertical orientation allows the cationic residues along the side of the protein to interact with the anionic headgroups. In the shallower orientation b, fewer hydrophobic residues reside in the membrane, but more cationic residues are able to interact with the anionic headgroups. Such snapshots are similar for the PDBu and ligand-free systems