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FEBS Lett. 2000 Apr 14;471(2-3):133-6.

Characterisation of calmodulin binding to cyclic nucleotide-gated ion channels from Arabidopsis thaliana.

Author information

1
Universität Freiburg, Institut für Biologie II, Zellbiologie, Schänzlestr. 1, D-79104, Freiburg, Germany.

Abstract

The recently identified cyclic nucleotide-gated ion channels (AtCNGCs) from Arabidopsis thaliana have the ability to bind calmodulin. Using two different methods, we mapped the binding site of AtCNGC1 to the last predicted alpha helix of the cyclic nucleotide binding domain. This is in contrast to CNGCs from animals, where the calmodulin binding site is located in the N-terminus, implying that different mechanisms for CNGC modulation have evolved in animals and plants. Furthermore, we demonstrate that AtCNGC1 and AtCNGC2 have different calmodulin binding affinities and we provide evidence for target specificities among calmodulin isoforms.

PMID:
10767408
DOI:
10.1016/s0014-5793(00)01383-1
[Indexed for MEDLINE]
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