Ellis S B, Williams M E, Ways N R, Brenner R, Sharp A H, Leung A T, Campbell K P, McKenna E, Koch W J, Hui A, Schwartz A, Harpold M M
Salk Institute Biotechnology/Industrial Associates, Inc., La Jolla, CA 92037.
Science. 1988 Sep 23;241(4873):1661-4. doi: 10.1126/science.2458626.
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.
互补DNA被分离出来,用于推导来自兔骨骼肌的二氢吡啶敏感、电压依赖性钙通道α1和α2亚基的一级结构。α1亚基含有钙拮抗剂的假定结合位点,是一种疏水蛋白,其序列与多个跨膜结构域一致,并与其他电压依赖性离子通道具有结构和序列同源性。相比之下,α2亚基是一种亲水蛋白,与其他已知蛋白质序列无同源性。核酸杂交研究表明,α1和α2亚基的mRNA以组织特异性方式差异表达,并且存在一个编码其他钙通道亚型的基因家族。