Visualizing structural transitions of ligand-dependent gating of the TRPM2 channel
作者： Ying Yin , Mengyu Wu , Allen L. Hsu , William F. Borschel , Mario J. Borgnia
DOI: 10.1101/516468
关键词:
摘要: The calcium-permeable transient receptor potential melastatin 2 (TRPM2) channel plays a key role in redox sensation many cell types. Channel activation requires binding of both ADP-ribose (ADPR) and Ca2+. recently published TRPM2 structures from Danio rerio the ligand-free ADPR/Ca2+-bound conditions represent closed open states, which uncover substantial tertiary quaternary conformational rearrangements. However, it is unclear how these rearrangements occur within tetrameric during gating. Here we report two cryo-electron microscopy same species complex with Ca2+ alone, ADPR Ca2+, determined to an overall resolution ~3.8 ~4.2 angstroms respectively. In comparison results, our studies capture two-fold symmetric intermediate offering glimpse structural transitions tetramer that bridge conformations.
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