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Acta Chimica Sinica ›› 2011, Vol. 69 ›› Issue (14): 1639-1644. Previous Articles Next Articles
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于辉,李卓,赵熹,黄旭日*
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YU Hui, LI Zhuo, ZHAO Xi, HUANG Xu-Ri
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Pentameric ligand-gated ion channels belong to an important family of membrane proteins and play key roles in physiological processes. Based on the X-ray structure of prokaryotic pentameric ligand-gated ion channels from Gloebacter violaceus (GLIC), we performed a total of 1.05 µs coarse-grained molecular simulations, combining with atomic-level molecular simulation, and observed the pore closure and corresponding quaternary twist. We found that the pore closure by a concerted motion of rotating-tilting (toward the pore) of helices M2. Combining with previous experimental results, a model of describing the conformational transition for channel gating process is derived from our simulations: the top of the M2 helix occurs large conformational fluctuations, followed by a global conformational changes of the whole subunit|this process passes from one subunit to the neighbor one, finally, leading to the entire channel conformational changes, such as a “chain-reaction”.
Key words: pentameric ligand-gated ion channel, gating, coarse-grained
YU Hui, LI Zhuo, ZHAO Xi, HUANG Xu-Ri. Multi-scale Molecular Simulations Study on the Gating Mechanism in a Pentameric Ligand-gated Ion Channel from Gloebacter Violaceus[J]. Acta Chimica Sinica, 2011, 69(14): 1639-1644.
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