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A mutation in the β interaction domain of the Ca 2+ channel α 1C subunit reduces the affinity of the (+)‐[ 3 H]isradipine binding site
Author(s) -
Hitzl Monika,
Striessnig Jörg,
Neuhuber Birgit,
Flucher Bernhard E.
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03054-5
Subject(s) - isradipine , beta (programming language) , protein subunit , alpha (finance) , g alpha subunit , mutation , chemistry , binding site , biophysics , domain (mathematical analysis) , stereochemistry , receptor , biology , biochemistry , medicine , gene , antagonist , mathematical analysis , mathematics , construct validity , nursing , computer science , patient satisfaction , programming language
The molecular mechanisms of how α 1 and β subunits of voltage‐gated Ca 2+ channels interact with one another are still controversial. Here we show that despite a mutation in the β interaction domain that has previously been shown to disrupt binding, α 1C Y467S and β 1a‐myc still formed immunoprecipitable complexes when coexpressed in tsA201 cells. However, the α 1C Y467S–β 1a‐myc complexes had a decreased affinity to (+)‐[ 3 H]isradipine. This indicates that the β interaction domain in the I–II loop of the α 1 subunit is not merely an anchor required for the functional interaction of the two Ca 2+ channel subunits but is itself part of the effector pathway for β‐induced channel modulation.