Article
A mutation in the beta interaction domain of the Ca(2+) channel alpha(1C) subunit reduces the affinity of the (+)-[(3)H]isradipine binding site.
FEBS letters - 31 Jul 2002
Hitzl Monika, Striessnig Jörg, Neuhuber Birgit, Flucher Bernhard E
Abstract excerpt
The molecular mechanisms of how alpha(1) and beta subunits of voltage-gated Ca(2+) channels interact with one another are still controversial. Here we show that despite a mutation in the beta interaction domain that has previously been shown to disrupt binding, alpha(1C)Y467S and beta(1a-myc) still formed immunoprecipitable complexes when coexpressed in tsA201 cells. However, the alpha(1C)Y467S-beta(1a-myc)...
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