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. Author manuscript; available in PMC: 2012 Jan 7.
Published in final edited form as: Cell. 2011 Jan 7;144(1):55–66. doi: 10.1016/j.cell.2010.12.013

Figure 2. The kinase catalytic domain and the NFD helix.

Figure 2

(A) Comparison of the NFD helix in the isolated PKCβII catalytic domain structure (grey) and the present full-length PKCβII structure, where the NFD helix and adjacent regions are colored cyan. (B) Close-up of the NFD region. (C) Comparison of the NFD region in full length PKCβII (cyan) and the ATP-bound kinase domain of PKCι (orange) (Takimura et al., 2010). (D) Sequence alignment of the NFD region of mammalian PKCs, PKCs from C. elegans and C. albicans (yeast), compared to AGC kinase family members PKA and Akt. An invariant proline corresponding to PKCβII Pro619 is at the start of the AGC-specific tail. The inactive NFD helix of our structure is indicated on the alignment (cyan box corresponds to helix in C), as are the rearranged, active NFD motifs of PKCι (orange boxes correspond to helices in C–D) and Akt2 (orange boxes).