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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
Language English Country United States
NLK
ScienceDirect (archiv)
from 1993-01-01 to 2009-12-31
- MeSH
- Amino Acid Motifs MeSH
- Financing, Organized MeSH
- Calmodulin metabolism MeSH
- TRPV Cation Channels genetics chemistry metabolism MeSH
- Rats MeSH
- Models, Molecular MeSH
- Solubility MeSH
- Structural Homology, Protein MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Animals MeSH
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.
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- $a Institute of Physiology, Academy of Sciences of the Czech Republic, Videnska 1083, 14220 Prague, Czech Republic.
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- $a 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.
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- $a kalmodulin $x metabolismus $7 D002147
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- $a kationtové kanály TRPV $x genetika $x chemie $x metabolismus $7 D050916
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- $t Biochemical & Biophysical Research Communications $w MED00009307 $g Roč. 375, č. 4 (2008), s. 680-683
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