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. Author manuscript; available in PMC: 2021 Jul 14.
Published in final edited form as: Immunity. 2020 Jun 17;53(1):106–114.e5. doi: 10.1016/j.immuni.2020.06.007

Figure 4. The hCASP1-mGSDMD interface plays an important role in their association.

Figure 4.

(A) Wild type or mutant GST-mGSDMD was used to pull down the hCASP1 (C285A) p22/p10 catalytic domain. The mutants harbor mutations of the exosite-binding residues in mGSDMD. Data shown are representative of three independent experiments.

(B) Wild type GST-mGSDMD was used to pull down hCASP1 catalytic domains harboring mutations such as C285A, W294A, I318E or K320E. Data shown are representative of three independent experiments.

See also Figure S4.