Figure 1.
Figure 1. Structure of Epac. a, Domain organization of Epac1
and 2. Indicated color code is used throughout the figure. b,
Stereo view of a 2F[o] - F[c] composite omitted electron density
map (contoured at 1.5 ).
The hydrophobic environment of Leu408 and Phe435 is shown.
Different parts of the peptide chain are highlighted by
individual colors. c, Ribbon diagram of the regulatory domain of
Epac2 with N and C termini as indicated. The C-terminal extra
helix of the DEP domain is dark green. d, Amino acid sequence,
with secondary structure annotation. The phosphate-binding
cassette (PBC) is indicated in red letters. Dashed lines
indicate portions of the polypeptide chain not visible in the
electron density. e, The two possible arrangements (1 and 2) for
the first cNMP-binding domain relative to the second (see text).
Arrangement 1 corresponds to (c). Dotted lines, linker 1 and 2,
indicate the minimal path of the polypeptide chain required to
bridge the gap in both arrangements.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2003,
10,
26-32)
copyright 2003.
).
The hydrophobic environment of Leu408 and Phe435 is shown.
Different parts of the peptide chain are highlighted by
individual colors. c, Ribbon diagram of the regulatory domain of
Epac2 with N and C termini as indicated. The C-terminal extra
helix of the DEP domain is dark green. d, Amino acid sequence,
with secondary structure annotation. The phosphate-binding
cassette (PBC) is indicated in red letters. Dashed lines
indicate portions of the polypeptide chain not visible in the
electron density. e, The two possible arrangements (1 and 2) for
the first cNMP-binding domain relative to the second (see text).
Arrangement 1 corresponds to (c). Dotted lines, linker 1 and 2,
indicate the minimal path of the polypeptide chain required to
bridge the gap in both arrangements.