Extended Data Fig. 10: Rationale for hybrid receptor design. | Nature

Extended Data Fig. 10: Rationale for hybrid receptor design.

From: A wheat resistosome defines common principles of immune receptor channels

Extended Data Fig. 10

a, Structural (top) and sequence (bottom) alignment of Sr35, HvMLA10, HvMLA13, TaSH1 and HvSH1. Amino acid 505 in the structurally and sequence conserved α4-helix of the WHD of Sr35 was included in hybrid CNL receptors. Structure of Sr35 is isolated from the cryo-EM Sr35 resistosome structure, while HvMLA10, HvMLA13, TaSH1 and HvSH1 were predicted using AlphaFold2. b, Structural alignment of Sr35 LRR (light blue) with structural prediction of TaSh1 (yellow) and c, HvSh1 (orange). d, Multiple protein sequence alignment of Sr35, TaSH1 and HvSH1. Circled amino acids were substituted to corresponding amino acids in the Sr35 sequence for the generation of TaSh1GOF and HvSh1GOF constructs. Amino acids highlighted in red and in red text are identical and possess similar properties, respectively.

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