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. Author manuscript; available in PMC: 2008 Aug 25.
Published in final edited form as: Biochemistry. 2006 Dec 5;45(51):15318–15326. doi: 10.1021/bi061701x

Figure 5. Structural Model of Epac1.

Figure 5

(A) Ribbon diagram of Epac1. The DEP, CBD, REM, RA, and CDC-25 homology domain are colored in pink, red, green, blue, and cyan, respectively. (B) The 31 hydrogen bonding network (dotted lines) of the switchboard, a five-strand, β-sheet like structure formed by the C-terminus of CBD (red), the N-terminus of the REM domain (green) and the loop of the helical hairpin of the catalytic core (cyan). (C) The hydrophobic core formed by the C-terminal helix of the helical hairpin of the catalytic core (cyan) and the REM domain (green). (D) Interactions between CBD and CDC-25 homology domain of Epac1. Hydrogen bonding and ionic interactions are shown with dotted and dash lines, respectively.