Structure of the sodium channel pore revealed by serial cysteine mutagenesis
Structure of the sodium channel pore revealed by serial cysteine mutagenesis
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DOI：
10.1073/pnas.93.1.300
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发表时间：
1996-01-09
影响因子：
11.1
通讯作者：
Tomaselli, GF
中科院分区：
文献类型：
--
作者：
PerezGarcia, MT;Chiamvimonvat, N;Tomaselli, GF
电压门控阳离子通道的孔由四个赋予选择性和导电性的膜内片段形成，关于这些关键的孔衬里或P片段的高级结构知之甚少。连续半胱氨酸诱变揭示了侧链可及性的模式，其与目前基于α-螺旋或β-链的有利结构模型相矛盾。与已知结构的许多酶的活性位点一样，钠通道孔由不规则环区域组成。
The pores of voltage-gated cation channels are formed by four intramembrane segments that impart selectivity and conductance, Remarkably little is known about the higher order structure of these critical pore-lining or P segments. Serial cysteine mutagenesis reveals a pattern of side-chain accessibility that contradicts currently favored structural models based on alpha-helices or beta-strands, Like the active sites of many enzymes of known structure, the sodium channel pore consists of irregular loop regions.