Extended Data Fig. 10: Structural analysis shows the basis for the specificity of DD adaptors for different receptors. | Nature

Extended Data Fig. 10: Structural analysis shows the basis for the specificity of DD adaptors for different receptors.

From: Electric dipole moment drives the dynamics of the TNFR1 complex I signalosome

Extended Data Fig. 10: Structural analysis shows the basis for the specificity of DD adaptors for different receptors.

a-b, Cryo-EM structure of Fas-FADD complex and its electrostatic potential surface. c, Calculated EDMs of the Fas-FADD complex. d-e, Structural modelling of TRAIL-R2-FADD complex and its electrostatic potential surface. f, Calculated EDMs of the TRAIL-R2-FADD complex. g-h, The “bottom” face of the TNFR1-DD pentamer has a negatively charged periphery, which complements the “top” face of the TRADD-DD pentamer. i-j, In the Fas-DD/FADD-DD complex, the “bottom” face of the Fas-DD pentamer shows charge complementation with the “top” face of the FADD-DD pentamer, which is incompatible with the “top” face of the TRADD-DD pentamer. k-l, Structural modelling of the DD pentamer DD from TRAIL-R2 or TRAIL-R1. The “bottom” faces of both receptors are compatible with the “top” face of the FADD-DD pentamer, but incompatible with TRADD-DD.

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