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. Author manuscript; available in PMC: 2012 Sep 6.
Published in final edited form as: Biochim Biophys Acta. 2009 Oct 29;1804(3):440–444. doi: 10.1016/j.bbapap.2009.10.017

Figure 2. The substrate peptide is positioned with respect to the αF-helix by a set of conserved hydrophobic residues in the Activation segment.

Figure 2

The phosphorylation site for a PKA substrate is shown as a yellow sphere. The hydrophobic pocket created by the P+1 loop is clearly anchored to the conserved W222 in the αF-helix via the APE-motif. The P-2 arginine forms a salt bridge with E230 in the C-terminus of the helix.