Van Andel Research Institute (VARI) scientists published an article in "Nature", revealing for the first time the atomic structure of TRPM2 protein that regulates core body temperature, mediates immune response, apoptosis, and programmed cell death.

"TRPM2 is absolutely necessary and critical for physical health. Unfortunately, we still lack important insights into its structure and mechanism of action until today," said Dr. Juan Du, assistant professor of VARI. "We hope that these findings will improve design. The urgently needed neurological disease drugs guide the way."

The atomic-level image of TRPM2 depicts a bell-like structure, with a transmembrane domain on the shoulder of the bell, and an extended NUDT9-H domain at the mouth of the bell. In addition, this study also pointed out a new drug binding site for ADPR, a signaling molecule related to oxidative stress and metabolism. This discovery overturned the previously believed that TRPM2 binds to ADPR in the NUDT9-H domain. The exact drug targets provide valuable details for the design of therapeutic drugs for body temperature-related diseases and the prevention of neuronal death during neurodegenerative diseases.

TRPM2 belongs to the TRP superfamily. This group of proteins mediates sensory stimuli such as pain, stress, vision, temperature, and taste. They are widely called ion channel proteins, nested in the cell membrane, and act as chemical agents for entering and leaving cells The gatekeeper of the signal.

TRPM2 protein may be a promising drug target for the treatment of oxidative stress-related neurological diseases (Alzheimer's disease and bipolar disorder, etc.) caused by chemical imbalance.

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