Extended Data Fig. 8: Comparison of the FAT-Kinase domain of mTORC1 in different states and the ATP position relative to other PIKKs. | Nature

Extended Data Fig. 8: Comparison of the FAT-Kinase domain of mTORC1 in different states and the ATP position relative to other PIKKs.

From: Structural basis for mTORC1 activation on the lysosomal membrane

Extended Data Fig. 8

a, The FAT (residues 1255–1453 are omitted) and kinase domains of the apo, soluble, intermediate, and fully active states of mTOR are shown side by side. The constriction between the FAT and kinase domain is indicated by double arrow curved lines. b, A close-up view of the ATP binding pocket of mTOR, superimposed by ATM and Mec1 based on the C-lobe (residues 2200–2400). The substrate of ATM, p53, is indicated with a red arrow.

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