Dissecting Intersubunit Contacts in Cyclic Nucleotide-Gated Ion Channels
Dissecting Intersubunit Contacts in Cyclic Nucleotide-Gated Ion Channels
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DOI：
10.1016/s0896-6273(02)00599-8
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发表时间：
2002-02
期刊：
影响因子：
16.2
通讯作者：
T. Rosenbaum;S. Gordon
中科院分区：
文献类型：
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作者：
T. Rosenbaum;S. Gordon
在环核苷酸门控（CNG）离子通道中，cGMP或cAMP的结合驱动构象变化，导致离子传导孔的打开。一个涉及配体结合与孔打开耦合的区域是C连接体区域。在这里，我们使用内源性半胱氨酸的交联来研究区域间的接近性。我们证明了一个单独的氨基酸- c481 -在每个相邻亚基的C连接区域可以形成一个二硫键。此外，使用串联二聚体，我们发现在n端区域的C35和C连接区域的C481之间的二硫键可以在亚基内或亚基之间形成。从我们的数据之间的接近的单个氨基酸和以前的研究，一个图片出现C连接作为一个潜在的二聚化界面。
In cyclic nucleotide-gated (CNG) ion channels, binding of cGMP or cAMP drives a conformational change that leads to opening of an ion-conducting pore. One region implicated in the coupling of ligand binding to opening of the pore is the C linker region. Here, we used crosslinking of endogenous cysteines to study interregion proximity. We demonstrate that an individual amino acid—C481—in the C linker region of each of two neighboring subunits can form a disulfide bond. Further, using tandem dimers, we show that a disulfide bond between C35 in the N-terminal region and C481 in the C linker region can form either within a subunit or between subunits. From our data on proximity between individual amino acids and previous studies, a picture emerges of the C linker as a potential dimerization interface.