Extended Data Fig. 7: Structural comparison between the intermediate and fully active states of mTOR. | Nature

Extended Data Fig. 7: Structural comparison between the intermediate and fully active states of mTOR.

From: Structural basis for mTORC1 activation on the lysosomal membrane

Extended Data Fig. 7

Structures are superimposed based on Rheb. a, A carton representation of the mTOR-Rheb-mLST8 subcomplex. The motion between intermediate and fully active states are indicated with lines that connect the backbone of both structures. The distance of the motion is labeled with a rainbow color. b, The soluble structure of mTORC1-Rheb is in between the conformational change of the intermediate and fully active states of mTORC1-Rheb on membrane. c, Only the fully active state contains the ordered loop in the backside of the ATP pocket. The ordered loop (904–920) is colored red.

Back to article page