| Literature DB >> 2458626 |
S B Ellis1, M E Williams, N R Ways, R Brenner, A H Sharp, A T Leung, K P Campbell, E McKenna, W J Koch, A Hui, A Schwartz, M M Harpold.
Abstract
Complementary DNAs were isolated and used to deduce the primary structures of the alpha 1 and alpha 2 subunits of the dihydropyridine-sensitive, voltage-dependent calcium channel from rabbit skeletal muscle. The alpha 1 subunit, which contains putative binding sites for calcium antagonists, is a hydrophobic protein with a sequence that is consistent with multiple transmembrane domains and shows structural and sequence homology with other voltage-dependent ion channels. In contrast, the alpha 2 subunit is a hydrophilic protein without homology to other known protein sequences. Nucleic acid hybridization studies suggest that the alpha 1 and alpha 2 subunit mRNAs are expressed differentially in a tissue-specific manner and that there is a family of genes encoding additional calcium channel subtypes.Entities:
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Year: 1988 PMID: 2458626 DOI: 10.1126/science.2458626
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728