Extended Data Fig. 3: Structural basis for the unique assembly of TNFR1-DD/TRADD-DD/RIPK1-DD ternary complex.
From: Electric dipole moment drives the dynamics of the TNFR1 complex I signalosome
a-e, Cartoon representation of the association between interfaces a and d of TNFR1-DD, TRADD-DD and RIPK1-DD, with interacting residues shown as sticks and interface a shown as electrostatic potential surface. f-j, Cartoon representation of the association between interfaces b and e among TNFR1-DD, TRADD-DD and RIPK1-DD, with interacting residues shown as sticks and interface b shown as electrostatic potential surface. k-o, Cartoon representation of the association between interfaces c and f among TNFR1-DD, TRADD-DD and RIPK1-DD, with interacting residues shown as sticks and interface c shown as electrostatic potential surface. p, Energetically favourable and unfavorable assembly pathways derived based on the calculated Gibbs free energy changes (ΔG) of pairwise interactions among TNFR1-DD, TRADD-DD and RIPK1-DD pentamer layers.
