6pkw
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Cryo-EM structure of the zebrafish TRPM2 channel in the apo conformation, processed with C2 symmetry (pseudo C4 symmetry)
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Structural highlights
FunctionTRPM2_DANRE Nonselective, voltage-independent cation channel that mediates Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels. Functions as ligand-gated ion channel. Binding of ADP-ribose to the cytoplasmic N-terminal region causes a conformation change; the channel is primed but still requires Ca(2+) binding to trigger channel opening.[1] References
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This page was last modified 09:26, 20 March 2024.