Fig. 3.

Fitting of Avo2 ankyrin repeats and Avo3 helices into TORC2. a TORC2 fitted with models for Avo2 ankyrin repeats (magenta), Avo3 helices (dark-green) and Tor2-Lst8 (colour coding as in Fig. 2). Boxes highlight the areas shown as close-up views in b–e. b Avo2 contacts loops formed by helices Nα18-Nα19 and Nα20-Nα21 of the Tor2 spiral (dark-blue). c Avo2 contacts FAT domain residues 1510–1513 (orange-yellow) of Tor2. d Two helices of Avo3 which likely are part of the armadillo-like helical domain contribute to the dimer interface by binding the Tor2 spiral of the other protomer. e Avo3 contacts helixes Nα27 and Nα29 of the adjacent Tor2 spiral. f Superimposition of the crystal structure of the human FKBP12-rapamycin-FRB complex (pdb ID: 1NSG) onto the Tor2 FRB domain, showing a clash between FKBP12 and Avo3. FKBP12 is shown in yellow and rapamycin in a stick representation. The transparent surface map is contoured at 7.5 sigma level