A novel homology model of TRPC3 reveals allosteric coupling between gate and selectivity filter
A novel homology model of TRPC3 reveals allosteric coupling between gate and selectivity filter
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DOI：
10.1016/j.ceca.2013.05.010
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发表时间：
2013-09-01
期刊：
影响因子：
4
通讯作者：
Groschner, Klaus
中科院分区：
文献类型：
--
作者：
Lichtenegger, Michaela;Stockner, Thomas;Groschner, Klaus
利用一个新的TRPC3分子模型，以Arcobacter buzleri(Na(V)AB)的电压门控钠通道为模板，进行了结构导向突变实验，以确定参与二价渗透和门控的氨基酸残基。在预测的选择性过滤器内的取代半胱氨酸可及性筛选发现，629-631氨基酸是渗透途径的最窄部分，估计的孔径为
Utilizing a novel molecular model of TRPC3, based on the voltage-gated sodium channel from Arcobacter butzleri (Na(V)AB) as template, we performed structure-guided mutagenesis experiments to identify amino acid residues involved in divalent permeation and gating. Substituted cysteine accessibility screening within the predicted selectivity filter uncovered amino acids 629-631 as the narrowest part of the permeation pathway with an estimated pore diameter of