title: Ionic interactions are essential for TRPV1 C-terminus binding to calmodulin.
abstract: Calmodulin (CaM) is known to play an important role in the regulation of TRP channels activity. Although it has been reported that CaM binds to the C-terminus of TRPV1 (TRPV1-CT), no classic CaM-binding motif was found in this region. In this work, we explored this unusual TRPV1 CaM-binding motif in detail and found that five residues from a putative CaM-binding motif are important for TRPV1-CT's binding to CaM, with arginine R785 being the most essential residue. The homology modelling suggests that a CaM-binding motif of TRPV1-CT forms an alpha helix that docks into the central cavity of CaM.
authors.affiliation: Institute of Physiology, Academy of Sciences of the Czech Republic, Videnska 1083, 14220 Prague, Czech Republic.
authors.forename: Lenka
authors.initials: L
authors.lastname: Grycova
authors.forename: Zdenek
authors.initials: Z
authors.lastname: Lansky
authors.forename: Eliska
authors.initials: E
authors.lastname: Friedlova
authors.forename: Veronika
authors.initials: V
authors.lastname: Obsilova
authors.forename: Hana
authors.initials: H
authors.lastname: Janouskova
authors.forename: Tomas
authors.initials: T
authors.lastname: Obsil
authors.forename: Jan
authors.initials: J
authors.lastname: Teisinger