Figure 3.
Ala substitutions at conserved residues disrupt RIC-3 interaction. (a) Sequence of L1-MX and MX peptides, and single and multiple site substitution peptides W347A, R349A, L353A, L1-MX-AAA, and L1-MX-7A. (b) Single-site substitution peptides W347A, R349A, or L353A in the MX helix preserve interaction with RIC-3, albeit with potentially altered affinity based on band intensities. (c and d) Multiple Ala substitutions in L1-MX-AAA and L1-MX-7A (two technical replicates) disrupt the interaction with RIC-3. RIC-3 band intensities are comparable to Cys-capped resin background. Data shows representative replicates of n ≥ 2 biological replicates and n ≥ 3 technical replicates; for L1-MX-AAA and RIC-3 assay, RIC-3 was extracted from a batch of 159 oocytes with n = 4 technical replicates. Source data are available for this figure: SourceData F3.

Ala substitutions at conserved residues disrupt RIC-3 interaction. (a) Sequence of L1-MX and MX peptides, and single and multiple site substitution peptides W347A, R349A, L353A, L1-MX-AAA, and L1-MX-7A. (b) Single-site substitution peptides W347A, R349A, or L353A in the MX helix preserve interaction with RIC-3, albeit with potentially altered affinity based on band intensities. (c and d) Multiple Ala substitutions in L1-MX-AAA and L1-MX-7A (two technical replicates) disrupt the interaction with RIC-3. RIC-3 band intensities are comparable to Cys-capped resin background. Data shows representative replicates of n ≥ 2 biological replicates and n ≥ 3 technical replicates; for L1-MX-AAA and RIC-3 assay, RIC-3 was extracted from a batch of 159 oocytes with n = 4 technical replicates. Source data are available for this figure: SourceData F3.

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