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. 2003 Dec 18;23(1):100–110. doi: 10.1038/sj.emboj.7600033

Figure 3.

Figure 3

Identification of MyD88 Death Domain residues required for the MyD88–Tube Interaction. (A) The Drosophila MyD88 polypeptide sequence is shown with the death domain (79–188, in blue) and the TIR domain (236–375, in green). Negatively charged residues (red) were changed to Lys; consecutive acidic residues were changed together. The interaction between these MyD88 mutants and the Tube death domain was assayed with anti-MyD88 immunoprecipitation essentially as described in Figure 2. Residues with mutations abolishing Tube binding (D113K, D163K, D166K, and D169K/D170K) are marked (∧). (B) Anti-MyD88 immunoprecipitation was used to compare the interaction of the Tube death domain with either wild-type MyD88 or the four indicated MyD88 mutants. (C) MyD88 initiated signaling as assayed with a Drosomycin–luciferase reporter. Wild-type or mutant forms of MyD88 as indicated, or the constitutively active form of Toll, Toll10B, were transfected into S2 cells together with pGL3–Drosomycin. The reporter assay was carried out as described in Materials and methods.