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α-螺旋中的拉链转变:生物膜中电压敏感离子通道门控的一种机制。

Zipper transition in an alpha-helix: a mechanism for gating of voltage-sensitive ion channels in a biological membrane.

作者信息

Clapp R E

出版信息

J Theor Biol. 1983 Sep 7;104(1):137-58. doi: 10.1016/0022-5193(83)90406-x.

DOI:10.1016/0022-5193(83)90406-x
PMID:6314058
Abstract

It is suggested that the gating currents which control the ion channels in a biological membrane are comprised of positive charges crossing the membrane along chains of hydrogen bonds. These chains are the sets of hydrogen bonds which hold alpha-helical protein segments in their rigid conformations. The passage of a positive charge in one direction along such a chain will convert hydrogen bonds from the usual rigid N--C = O...H--N form to a flaccid N = C--O--H...N form. This "zipper" transition can be reversed by the passage of the positive charge along the return route. A flaccid protein rod can clog an ion channel and thereby close it. When all of the protein rods framing an ion channel are in the rigid conformation, the channel is open. This mechanism is used to explain some of the observed characteristics of calcium ion channels and sodium ion channels.

摘要

有人提出,控制生物膜中离子通道的门控电流由沿着氢键链穿过膜的正电荷组成。这些链是将α-螺旋蛋白片段保持在其刚性构象的氢键集合。正电荷沿这样一条链的一个方向通过会使氢键从通常的刚性N--C = O...H--N形式转变为松弛的N = C--O--H...N形式。这种“拉链”转变可以通过正电荷沿返回路径通过而逆转。松弛的蛋白棒会堵塞离子通道,从而使其关闭。当构成离子通道的所有蛋白棒都处于刚性构象时,通道是开放的。该机制用于解释钙离子通道和钠离子通道的一些观察到的特性。

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J Theor Biol. 1983 Sep 7;104(1):137-58. doi: 10.1016/0022-5193(83)90406-x.
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