Ionic interactions are essential for TRPV1 C-terminus binding to calmodulin

. 2008 Oct 31 ; 375 (4) : 680-3. [epub] 20080826

Jazyk angličtina Země Spojené státy americké Médium print-electronic

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/pmid18755153
Odkazy

PubMed 18755153
DOI 10.1016/j.bbrc.2008.08.094
PII: S0006-291X(08)01626-4
Knihovny.cz E-zdroje

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

Najít záznam

Citační ukazatele

Nahrávání dat ...

Možnosti archivace

Nahrávání dat ...