Scientists at the Van Andel Institute (VARI) have for the first time revealed the atomic structure of the protein TRPM2, which regulates core body temperature, mediates immune responses, and apoptosis, programmed cell death.
TRPM2 is part of the TRP superfamily, which mediates sensory stimuli such as pain, stress, vision, temperature, and taste. They are widely known as ion channel proteins, nested within the cell membrane, and act as chemistry into and out of cells. The gatekeeper of the signal. The eight proteins that make up the TRPM superfamily are part of this broader group.
TRPM2 protein may be a promising drug target for the treatment of oxidative stress-related neurological diseases (Alzheimer's and bipolar disorder, etc.) caused by chemical imbalances.
The atomic image of TRPM2 depicts a bell-like structure with a transmembrane domain on the shoulder of the clock and an extended NUDT9-H domain at the bell. In addition, the study also identified a new drug-binding site for ADPR, a signaling molecule involved in oxidative stress and metabolism, a finding that reversed the previously identified view that TRPM2 binds to ADPR in the NUDT9-H domain. The exact drug targets provide valuable details for designing treatments for body temperature-related diseases and preventing neuronal death during neurodegenerative diseases.
"Although we know that TRPM2 is a component of many important life processes and potential drug targets, we are not sure what it looks like or how it works," the researchers said. “Today's discovery has changed all of this and helped to understand this extremely important molecule more fully.”
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