生命科学联合中心学术报告

题目：Structure of a mammalian ryanodine receptor.

报告人：Andrew R. Marks, M.D.

Wu Professor  and Chair, Department of Physiology and Cellular Biophysics

Founding Director, Helen and Clyde Wu Center for Molecular Cardiology

Columbia University College of Physicians & Surgeons

时间：2015-11-19（周四），13:00-14:30pm

地点：北京大学邓祐才报告厅

联系人：汪阳明  北大-清华生命科学联合中心

RyR channels are required for release of calcium from intracellular stores, a process essential for many cellular functions including excitation-contraction (EC) coupling in skeletal and cardiac muscle, and hormone and neurotransmitter release.  They are amongst the largest ion channels, comprised of the four identical ~565 kDa channel-forming protomers, as well as regulatory subunits, enzymes and their respective targeting/anchoring proteins, in a macromolecular complex that exceeds three million daltons. We have obtained high-resolution cryo-electron microscopy (Cryo-EM) reconstructions from highly purified rabbit skeletal muscle RyR1 in the open and closed states. Our data reveal that RyRs are members of the six transmembrane family of ion channels and show a mechanism for channel gating that couples a change in the conformation of the calcium binding site directly to opening of the channel pore, suggesting that calcium binding facilitates mechanical coupling of conformational changes in the cytosolic region to opening of the channel gate. The channel-specific ligand ryanodine shows the channel to be locked in an open state consistent with the know effects of ryanodine on the single channel properties of RyR1. We have mapped disease causing mutations on the structure proving insight regarding disease mechanisms for arrhythmias and muscular dystrophies.

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