Zervamicins, a structurally characterised peptide model for membrane ion channels.
Zervamicins, a structurally characterised peptide model for membrane ion channels.
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Zervamicins，一种膜离子通道结构特征肽模型。
DOI：
10.1016/s0006-291x(05)80768-5
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发表时间：
1992
影响因子：
3.1
通讯作者：
Balaram,P
中科院分区：
文献类型：
--
作者：
Agarwalla,S;Mellor,IR;Sansom,MS;Karle,IL;Flippen-Anderson,JL;Uma,K;Krishna,K;Sukumar,M;Balaram,P
电压依赖性膜通道由zervamicins形成，zervamicins是一组含有α-氨基异丁酸的肽。极性残基如Thr、Gln和Hyp在促进螺旋束形成中的作用通过合成非极性类似物的通道寿命显著降低来建立。Leu 1-泽维霉素的晶体结构显示弯曲螺旋的缔合。凸面之间的极性接触导致具有中心收缩的水通道的“沙漏”状布置。结构表明，门控机制可能涉及运动的Gln 11羧酰胺基团。Gln 3可能在调节通道口大小方面起一定作用。
Voltage dependent membrane channels are formed by the zervamicins, a group of α-aminoisobutyric acid containing peptides. The role of polar residues like Thr, Gln and Hyp in promoting helical bundle formation is established by dramatically reduced channel lifetimes for a synthetic apolar analog. Crystal structures of Leu1-zervamicin reveal association of bent helices. Polar contacts between convex faces result in an ‘hour glass’ like arrangement of an aqueous channel with a central constriction. The structure suggests that gating mechanisms may involve movement of the Gln11carboxamide group. Gln3may play a role in modulating the size of the channel mouth.