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首页> 外文期刊>Neuron >Structural analysis of the voltage-dependent calcium channel beta subunit functional core and its complex with the alpha 1 interaction domain.
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Structural analysis of the voltage-dependent calcium channel beta subunit functional core and its complex with the alpha 1 interaction domain.

机译：电压依赖性钙通道β亚基功能核心及其与alpha 1相互作用域的复合物的结构分析。

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摘要

Voltage-dependent calcium channels (VDCC) are multiprotein assemblies that regulate the entry of extracellular calcium into electrically excitable cells and serve as signal transduction centers. The alpha1 subunit forms the membrane pore while the intracellular beta subunit is responsible for trafficking of the channel to the plasma membrane and modulation of its electrophysiological properties. Crystallographic analyses of a beta subunit functional core alone and in complex with a alpha1 interaction domain (AID) peptide, the primary binding site of beta to the alpha1 subunit, reveal that beta represents a novel member of the MAGUK protein family. The findings illustrate how the guanylate kinase fold has been fashioned into a protein-protein interaction module by alteration of one of its substrate sites. Combined results indicate that the AID peptide undergoes a helical transition in binding to beta. We outline the mechanistic implications for understanding the beta subunit's broad regulatory role of the VDCC, particularly via the AID.
机译：电压依赖性钙通道（VDCC）是多蛋白装配，可调节细胞外钙进入电刺激细胞的进入并充当信号转导中心。 alpha1亚基形成膜孔，而细胞内β亚基负责通道向质膜的运输并调节其电生理特性。单独和与α1相互作用域（AID）肽（β与α1亚基的主要结合位点）复合的β亚基功能核心的晶体学分析表明，β代表MAGUK蛋白家族的一个新成员。这些发现说明了鸟苷酸激酶折叠是如何通过改变其底物位点之一而形成蛋白质-蛋白质相互作用模块的。综合结果表明，AID肽在与β结合时经历了螺旋过渡。我们概述了了解VDCC的β亚基的广泛调节作用的机理，特别是通过AID。

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