Ionic interactions are essential for TRPV1 C-terminus binding to calmodulin.
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.
Grycova
Lenka
L
Institute of Physiology, Academy of Sciences of the Czech Republic, Videnska 1083, 14220 Prague, Czech Republic.
Lansky
Zdenek
Z
Friedlova
Eliska
E
Obsilova
Veronika
V
Janouskova
Hana
H
Obsil
Tomas
T
Teisinger
Jan
J