|
Figure 3.
Figure 3. Substrate Binding by IP[3]-3K(A) A view of the
active site showing the ATP analog and Ins(1,4,5)P[3] bound to
the enzyme. The subdomains and motifs are colored as in Figure
1. Side chains interacting with the ligands are shown as sticks
and ligand-bound water molecules as white spheres.(B) A
schematic of the interactions with the ligands made with
LIGPLOT.(C) A surface illustration of the IP[3]-3K catalytic
domain colored by electrostatic potential with negatively
charged regions red and positive blue. The bound AMPPNP is shown
as green sticks and the Ins(1,4,5)P[3] as yellow sticks.(D) A
close-up of the ATP binding pocket in the presence of AMPPNP
(left) and in its absence (right), showing Trp188 and His194
from the putative auto-inhibitory region mimicking the
interactions formed by ATP.
|