Fox Chase Cancer Center researchers and their colleagues in Japan and San Francisco have obtained new insight into the molecular structure of prion particles responsible for mad cow disease and other degenerative neurological disorders. In new research to be published in this weeks Online Early Edition of the Proceedings of the National Academy of Sciences (www.pnas.org), Fox Chase biophysicist Heinrich Roder, Ph.D., and colleagues describe a computer model of the structural core of prions, based on biophysical measurements of a fibrous form of a prion protein fragment. Prions are infectious protein particles linked to degenerative neurological diseases in animals and humans, such as mad cow disease (bovine spongiform encephalopathy or BSE) in cattle, scrapie in sheep and goats, and Creutzfeldt-Jakob disease (CJD) in humans.
For proteins, form really does equal function. Not only are they essential building blocks of the body, but proteins are also the workers of every cell, carrying out its specific functions. This function depends on the ultimate three-dimensional shape of the protein, a form achieved by folding flexible chains of amino acids until each is properly aligned so that the protein can do its job. Normally, the folding of proteins is highly efficient and specific, but sometimes the process goes awry, resulting in dangerous misfolded forms.
Prion diseases result from the conversion of a normal cellular protein into an alternative structure that forms threadlike fibers called amyloid fibrils. They accumulate in target tissues, such as brain tissue, where they cause the progressive degeneration of cognitive and motor functions and ultimately prove fatal.
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