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Chemistry of cation hydration and conduction in a skeletal muscle ryanodine receptor

By Zhaolong Wu, Congcong Liu, Hua Yu, Duan Kang, Yinping Ma, Xuemei Li, Lei Zhang, Chun Fan, Xin-Zheng Li, Chen Song, Chang-Cheng Yin, Youdong Mao

Posted 11 Aug 2019
bioRxiv DOI: 10.1101/732172

Ryanodine receptors (RyRs) are Ca2+-regulated Ca2+ channels of 2.2-megadalton in muscles and neurons for calcium signaling. How Ca2+ regulates ion conduction in the RyR channels remains elusive. We determined a 2.6-Å cryo-EM structure of rabbit skeletal muscle RyR1, and used multiscale dynamics simulations to elucidate cation interactions with RyR1. We investigated 21 potential cation-binding sites that may together rationalize biphasic Ca2+ response of RyR1. The selectivity filter captures a cation hydration complex by hydrogen-bonding with both the inner and outer hydration shells of water molecules. Molecular dynamics simulations suggest that adjacent Ca2+ ions moving in concert along ion-permeation pathway are separated by at least two cation-binding sites. Our analysis reveals that RyR1 has been evolved to favor its interactions with two hydration shells of cations.

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