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Figure 1.
Figure 1: Active Epac 2. a, Domain organization of Epac2.
Residues that were subjected to mutational analysis are
indicated. The same colour code is used throughout the figures.
Hinge (residues 432–445, dark green); helical hairpin
(residues 906 to 946, dark blue). CDC25-HD, CDC25 homology
domain; CNB, cyclic nucleotide binding domain; DEP, Dishevelled,
Egl-10, Pleckstrin domain; RA, Ras-association domain; REM,
Ras-exchange motif. b, Left, inactive Epac2 (first CNB and DEP
domain omitted); right, active Epac2  305
 Sp-cAMPS
RAP1B.
RAP1B is shown orange; Sp-cAMPS and SO[4]^2- are shown in ball
and stick representation. Arrow, movement of the second CNB
domain; straight lines, missing connectivity; dotted lines,
ionic latch (IL); asterisks, interface between the REM and the
CNB domain; HP, helical hairpin; PBC, phosphate binding
cassette. c, RAP1B placed into the inactive structure. d, The
crystal structure of Epac2 305
Sp-cAMPS
RAP1B
was fitted into the EM density reconstruction (grey grid) of
full length Epac2 cAMP
RAP1B.
Yellow surface, difference density.
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