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

L. Grycova, Z. Lansky, E. Friedlova, V. Obsilova, H. Janouskova, T. Obsil, J. Teisinger

Research output: Contribution to JournalArticleAcademicpeer-review

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 languageEnglish
Pages (from-to)680-683
JournalBiochemical and Biophysical Research Communications
Volume375
Issue number4
DOIs
Publication statusPublished - 2008

Bibliographical note

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

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