Richards Mark W, Butcher Adrian J, Dolphin Annette C
Laboratory of Cellular and Molecular Neuroscience, Department of Pharmacology, University College London, London WC1E 6BT, UK.
Trends Pharmacol Sci. 2004 Dec;25(12):626-32. doi: 10.1016/j.tips.2004.10.008.
It has taken 17 years from the first identification of a voltage-gated Ca2+ channel (CaV) beta-subunit as a band on a gel following purification of skeletal muscle dihydropyridine (DHP) receptors in 1987 to the publication of key information on the structures of Ca2+ channel beta-subunits. Three recent X-ray crystallographic studies have now solved the structures of the core domains of three Ca2+ channel beta-subunits. In this article, the properties of these cytoplasmic auxiliary subunits will first be summarized. Then the CaVbeta structures and the information they provide regarding how these proteins interact with the CaValpha1 subunit will be discussed and the possible implications of these new data for G-protein modulation of Ca2+ channels will be examined.
从1987年首次鉴定出电压门控Ca2+通道（CaV）β亚基是骨骼肌二氢吡啶（DHP）受体纯化后凝胶上的一条带，到关于Ca2+通道β亚基结构的关键信息发表，历时17年。最近的三项X射线晶体学研究现已解析出三种Ca2+通道β亚基核心结构域的结构。在本文中，将首先总结这些胞质辅助亚基的特性。然后将讨论CaVβ结构以及它们提供的关于这些蛋白质如何与CaVα1亚基相互作用的信息，并研究这些新数据对Ca2+通道G蛋白调节的可能影响。
