Interaction of ions with the luminal sides of wild-type and mutated skeletal muscle ryanodine receptors

Roman Schilling, Rainer H.A. Fink, Wolfgang B. Fischer*

*此作品的通信作者

研究成果: Article同行評審

3 引文 斯高帕斯(Scopus)

摘要

Ryanodine receptors (RyRs) are the largest known ion channels, and are of central importance for the release of Ca2+ from the sarco/endoplasmic reticulum (SR/ER) in a variety of cells. In cardiac and skeletal muscle cells, contraction is triggered by the release of Ca2+ into the cytoplasm and thus depends crucially on correct RyR function. In this work, in silico mutants of the RyR pore were generated and MD simulations were conducted to examine the impact of the mutations on the Ca2+ distribution. The Ca2+ distribution pattern on the luminal side of the RyR was most affected by G4898R, D4899Q, E4900Q, R4913E, and D4917A mutations. MD simulations with our wild-type model and various ion species showed a preference for Ca2+ over other cations at the luminal pore entrance. This Ca2+-accumulating characteristic of the luminal RyR side may be essential to the conductance properties of the channel.

原文English
文章編號37
期刊Journal of Molecular Modeling
22
發行號1
DOIs
出版狀態Published - 1月 2016

指紋

深入研究「Interaction of ions with the luminal sides of wild-type and mutated skeletal muscle ryanodine receptors」主題。共同形成了獨特的指紋。

引用此