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[Preprint]. 2023 Jun 16:rs.3.rs-3026818. [Version 1] doi: 10.21203/rs.3.rs-3026818/v1

Fig. 7. Structural model of CCDC22-CCDC93 binding to COMMD.

Fig. 7.

(A-C) Overlay of all 25 AlphaFold Multimer models and schematic showing COMMD decamer ring binding to CCDC22-CCDC93, with (A) highlighting the central ring of the COMM domain, (B) highlighting the globular domains on the two sides of the ring, and (C) highlighting the conformation of CCDC22 and CCDC93 CBDs. (D) Interaction surface between the COMMD ring (surface representation) with CCDC22-CCDC93 CBDs (cartoon). Key interactions are shown as sticks and polar interactions are represented with a dashed yellow line. Residues mutated in this study are outlined with a black box. (E) Immunoprecipitation of CCDC22 carrying indicated point mutations expressed in HEK293T cells and immunoblotting for the indicated proteins.