Abstract
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. © 2008 Elsevier Inc. All rights reserved.
Original language | English |
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Pages (from-to) | 680-683 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 375 |
Issue number | 4 |
DOIs | |
Publication status | Published - 2008 |