Understanding how the brain processes bitter, umami, and sweet tastes might sooner or later help researchers design more effective medication for neurological disorders.
Scientists from Van Andel Institute have, for the first time, revealed the close to the atomic-level structure of a calcium homeostasis modulator (CALHM), a type of protein that performs crucial roles in processing style stimuli and mitigating toxicity in brain cells. These proteins work by sensing chemical and electrical modifications of their environment—within the taste buds, for instance—and relaying the information back to the brain.
Additionally, they help regulate calcium concentrations and amyloid-beta protein levels within the central nervous system. Previous analysis has proven that irregular changes in CALHMs—and the resulting dysregulation of calcium or build-up of amyloid-beta—can contribute to Alzheimer’s disease, stroke, and different neurological conditions.
The shape of a protein is a key factor in how that protein carries out its function, very like how a particular key only works with a certain lock. Within the case of CALHM2, the new pictures show drastic variations in its structure when it’s in its open state versus its inhibited state, offering new perception into how the protein works in varying circumstances.
Importantly, the group additionally recognized an area of the protein that may be an optimal drug target.
The findings have been made possible by VAI’s state-of-the-art David Van Andel Advanced Cryo-Electron Microscopy Suite, which permits scientists to view a few of life’s smallest parts in exquisite detail. VAI’s most powerful microscope, the Titan Krios, can visualize molecules 1/10,000th the width of a human hair.