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Figure 3.
Figure 3: PDE bold gamma- /
alpha- [t/i1]
interactions. a,  A-weighted
2F[o] - F[c] electron density map for  [t/i1]
 GDP
AlF^-[4]
PDE
 RGS9
(1.5 ).
Anomalous difference Fourier density (15 )
in coral. b, Intermolecular contact (sub 4 Å) matrix for PDE
residues
(orange) that contact [t/i1]
non-switch residues (green) or [t/i1]
switch residues (blue). Electrostatic interactions to side
chains are shown in red, to main chain in green. van der Waals
contacts to side chains, to main chain or to both are shown in
black, grey and lavender, respectively. Water-mediated
interactions are indicated by blue circles. The root-mean-square
deviation (rmsd) for [t/i1]
contact residues (C atoms
are in black, overall side-chain deviation in grey) is shown for
[t/i1]
RGS9
versus [t]
GTP
S
(left)6 and [t]
GDP
AlF^-[4]
(right)8. Results of PDE alanine
scanning mutagenesis on GTPase stimulation (light-green bars)
and K[A] (dark-blue bars; ref. 13) are shown above. c, C trace
of PDE [50
-87]. C atoms
of residues contacting [t/i1]
switch II, the 3/
3
-  5
loop region or both are in blue, green and orange, respectively.
d, CPK representation of PDE W70
in the switch II/ 3
groove with residues that contact W70 in orange. e, Diagram of
PDE /switch
II/RGS9 interactions coloured as in a. f, CPK representation of
the heterotrimeric complex with the five C-terminal amino acids
of PDE in
red.
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