Ionic interactions are essential for TRPV1 C-terminus binding to calmodulin
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
18755153
DOI
10.1016/j.bbrc.2008.08.094
PII: S0006-291X(08)01626-4
Knihovny.cz E-zdroje
- MeSH
- aminokyselinové motivy MeSH
- kalmodulin metabolismus MeSH
- kationtové kanály TRPV chemie genetika metabolismus MeSH
- krysa rodu Rattus MeSH
- molekulární modely MeSH
- rozpustnost MeSH
- strukturní homologie proteinů MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- kalmodulin MeSH
- kationtové kanály TRPV MeSH
- Trpv1 protein, rat MeSH Prohlížeč
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.
Citace poskytuje Crossref.org
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Calmodulin and S100A1 protein interact with N terminus of TRPM3 channel