Fig. 5: PP2A:B55 recruitment.
From: Cryo-EM structures of PP2A:B55–FAM122A and PP2A:B55–ARPP19
a, PP2A:B55 SHELM sequences from experimentally confirmed B55 interactors. b, Left, 2D 1H,15N HSQC spectrum of 15N-labelled p107 alone and with B55LL (p107:B55 ratio is shown). Right, 2D 1H,15N HSQC spectrum of 15N-labelled p107 alone and with B55LL and an excess of unlabelled FAM122A (p107:B55:FAM122ANterm ratio is shown). c, Model of FAM122A-mediated displacement of p107. d, Overlay of PP2A:B55 bound to tpARPP19 or FAM122A. e, Magnified view of the overlapping regions shown in d. f, Overlay of tpARPP19 (orange) or FAM122A (magenta) at the B55 platform. g, Overlay of tpARPP19 (orange) or FAM122A (magenta) at the PP2Ac catalytic pocket. PP2Ac residues from the ARPP19 complex are labelled in cyan and those from the FAM122A complex are labelled in grey. Ionic interactions are shown as dashed lines. Metal ions in PP2Ac are shown as spheres. h, 2D 1H,15N HSQC spectrum of 15N-labelled FAM122A with and without B55LL. i, 2D 1H,15N HSQC spectrum of 15N-labelled FAM122A with and without B55LL and unlabelled tpARPP19. j, Model of FAM122A and ARPP19 binding B55LL simultaneously.
