Ionic interactions are essential for TRPV1 C-terminus binding to calmodulin.

Lenka Grycova1, Zdenek Lansky, Eliska Friedlova

  • 1Institute of Physiology, Academy of Sciences of the Czech Republic, Videnska 1083, 14220 Prague, Czech Republic.

Summary

Calmodulin (CaM) binding to TRPV1 channels is crucial for TRP channel regulation. This study identifies key residues, including R785, within an unusual TRPV1 C-terminal motif essential for CaM interaction.

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