Ionic interactions are essential for TRPV1 C-terminus binding to calmodulin
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
18755153
DOI
10.1016/j.bbrc.2008.08.094
PII: S0006-291X(08)01626-4
Knihovny.cz E-resources
- 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
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.
References provided by Crossref.org
Characterization of the S100A1 protein binding site on TRPC6 C-terminus
Integrative binding sites within intracellular termini of TRPV1 receptor
PtdIns(4,5)P2 interacts with CaM binding domains on TRPM3 N-terminus
Calmodulin and S100A1 protein interact with N terminus of TRPM3 channel
