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Architecture of the human TRPM2 channel

Structural Biology
Adenosine diphosphate–ribose (ADPR) mediates calcium (Ca2+) release by activating the transient receptor potential melastatin 2 (TRPM2) channel. Three structures now elucidate the conformational regulation mechanism of TRPM2 gating. Wang et al. describe cryo–electron microscopy structures of human TRPM2 in the apo, ADPR-bound, and ADPR- and Ca2+-bound states. In the apo state, both intra- and intersubunit interactions appeared to lock TRPM2 into a closed and autoinhibited state. ADPR binding disrupted some interactions and dramatically altered the TRPM2 conformation. Binding of Ca2+ further primed the opening of the channel.

Science , this issue p. [eaav4809][1]

 [1]: /lookup/doi/10.1126/science.aav4809