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Figure 5—figure supplement 6.

ID: ZDB-IMAGE-210319-20
Publication: Vinayagam et al., 2020 - Structural basis of TRPC4 regulation by calmodulin and pharmacological agents
All Figures: Figures for Vinayagam et al., 2020

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Figure Caption

Figure 5—figure supplement 6. Biochemical and structural analysis of CaM N- and C-lobe binding to TRPC4.

(A) SDS gel electrophoresis analysis of TRPC4 binding to MBP-fused N- and C-lobes of CaM after a pull-down assay using amylose resin. Lane M - protein size marker, lane 1 - TRPC4 input, lane 2 - flow through, lane 3 - wash and lane 4 - elution fractions of corresponding N- and C-lobes of CaM. (B) Superposition of the N- (light blue) and C-lobe (wheat) of CaM-bound to TRPC4 (light green). The CaM residues predicted to interact with TRPC4 are shown in stick representation with the labels colored according to the lobe. (C). Superposition of the N- and C-lobe of CaM-bound to TRPC4. The CaM residues predicted to interact with TRPC4 are colored based on the sequence conservation.

Acknowledgments

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