文章基本信息

标题：Structural insights into neuronal K+ channel–calmodulin complexes
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作者：Karen Mruk ; Shiven M.D. Shandilya ; Robert O. Blaustein 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2012
卷号：109
期号：34
页码：13579-13583
DOI：10.1073/pnas.1207606109
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Calmodulin (CaM) is a ubiquitous intracellular calcium sensor that directly binds to and modulates a wide variety of ion channels. Despite the large repository of high-resolution structures of CaM bound to peptide fragments derived from ion channels, there is no structural information about CaM bound to a fully folded ion channel at the plasma membrane. To determine the location of CaM docked to a functioning KCNQ K+ channel, we developed an intracellular tethered blocker approach to measure distances between CaM residues and the ion-conducting pathway. Combining these distance restraints with structural bioinformatics, we generated an archetypal quaternary structural model of an ion channel-CaM complex in the open state. These models place CaM close to the cytoplasmic gate, where it is well positioned to modulate channel function.
关键词：KCNQ2 ; KCNQ3 ; M-current ; calmodulation ; tetraethylammonium