The tiny protein known as transthyretin can cause big problems in the body when it misfolds after secretion.
Scripps Research InstituteJan 29 2025 While healthy transthyretin moves hormones through blood and spinal fluid, misfolded versions of the protein form dangerous clumps in the heart and along nerves-triggering a progressive and fatal disease known as transthyretin amyloidosis . Up to a quarter of all men over the age of 80 have some degree of ATTR, which can cause shortness of breath, dizziness and tingling or loss of sensation in the extremities.
The new structures reveal differences in two thyroid hormone binding sites previously thought to be identical, and help explain why a drug binding to one site changes the ability of drugs to bind the opposing site." Another method, cryo-electron microscopy , flash-freezes proteins to catch them in their more natural structures. However, these frozen proteins are then suspended in a liquid and small proteins like transthyretin tend to get stuck at the air-liquid boundary rather than remaining fully submerged. This affects both the proteins' structural stability and the ability to illuminate their detailed structure.
Related StoriesWhen the team tested the approach with transthyretin, they discovered that transthyretin forms asymmetric structures with two differently shaped binding pockets. Based on the more than 200 crystal structures that had been solved in the past, these binding sites had been assumed to be identical.
Amyloidosis Blood Drugs Heart Hormone Molecular Biology Molecule Research
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