Extended Data Fig. 7: Comparison of the inhibitory conformations of PI3Ks.
From: Structural basis of phosphatidylinositol 3-kinase C2α function
(a) Auto-inhibited conformation of PI3Kγ (pdb: IE8X). kα12 (red) bends inward towards the catalytic pocket. (b) Auto-inhibited conformation of yeast Vps34/Vps15 in complex II (pdb: 5DFZ). The activation loop of VPS34 (yellow) is locked by kα12 (red) and the N-terminus of VPS15 (blue). (c) Auto-inhibited conformation of PI3KC2αΔN as ribbon and surface representation. The distal C2 domain binds to the RBD. The yellow and orange regions represent the catalytic pocket and the activation loop, where lipid substrates bind. The PI(4,5)P2-binding surface in the distal C2 domain is colored in blue. The locations of the lipid-binding pockets are distributed on different sides of the PI3KC2α molecule in the closed conformation.
