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.

• MeSH
• Amino Acid Motifs MeSH
• Calmodulin metabolism   MeSH
• TRPV Cation Channels chemistry   genetics   metabolism   MeSH
• Rats MeSH
• Models, Molecular MeSH
• Solubility MeSH
• Structural Homology, Protein MeSH
• Animals MeSH
• Check Tag
• Rats MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Calmodulin MeSH
• TRPV Cation Channels MeSH
• Trpv1 protein, rat MeSH Browser