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News

First look at the atomic structure of a protein linked to alzheimer's disease

Yale University : 18 September, 2004  (New Product)
'Alzheimer's disease is a major health problem because of the aging of the population,' said the principal investigator, Ya Ha, assistant professor of pharmacology at Yale School of Medicine. 'Very little is known about the mechanism of the disease and there currently is no cure and no effective treatment.'
In a paper published this month in Molecular Cell, Yale researchers have, for the first time, described the atomic structure of a protein linked to Alzheimer's disease.

'Alzheimer's disease is a major health problem because of the aging of the population,' said the principal investigator, Ya Ha, assistant professor of pharmacology at Yale School of Medicine. 'Very little is known about the mechanism of the disease and there currently is no cure and no effective treatment.'

Rare mutations of human amyloid precursor protein are known to cause Alzheimer's disease at an early age in a very small percentage of the population. Since that link was made, researchers have attempted to determine the function of APP and how it converts to a smaller protein, amyloid beta-peptide. Amyloid beta-peptide, which is derived from APP, forms neuronal and vascular amyloid deposits in Alzheimer's disease.

Using X-ray crystallography, Ha and Yongcheng Wang, a postdoctoral research scientist in his laboratory, observed an unusual structural feature of APP. They found that APP consists of two long rod-like molecules that form a very tight complex, and, surprisingly, with the head of one molecule touching the tail of the other.

'That observation suggested a novel possibility, that APP may function to mediate cell-to-cell contact by interacting with itself, a process known as homophilic binding,' Ha said.

By functioning as its own binding partner, the APP from neighboring cells may thus affect the proteolytic processes that convert APP to the neurotoxic amyloid beta-peptide, Ha said. Such a partner, long thought to be a different protein, has never been previously found, he said.
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