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Figure 4.
Figure 4: C-linker interactions and cyclic nucleotide-dependent
tetramer formation. a, Stereoview of intersubunit C-linker
contacts. Helices A' and B' of one protomer are in red, and
helices C' and D' of an adjacent protomer are in blue. b, HCN2I
sedimentation equilibrium data in the absence (top) and presence
(bottom) of cAMP. The measurements and the models used to fit
the experimental data are shown as open yellow circles and thin
black lines, respectively. The thick black, red and blue lines
represent, respectively, the proportion of monomer, dimer and
tetramer calculated from the models. The residuals are shown for
a monomer -dimer (red) or a monomer -dimer -tetramer (blue)
model (top), and for a monomer -dimer (red) or a monomer
-tetramer (blue) model (bottom). c, Cartoon of an unliganded
closed channel (left) and a liganded open channel (right).
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