Scientists have toiled well over a decade trying to determine the structure of huntingtin, one of nine polyglutamine (polyQ)-containing proteins known to cause neurodegenerative disease when misfolded forms of the molecule aggregate in the brain. The current study unveils the first crystal structure of a polyQ-expanded protein (>Q10) in its native context. Seven was the magic number in this technological tour de force. “Because the structure itself is not well formed, it was very difficult to make the crystals, and the x-ray diffraction was very complicated,” Kim told ARF. “That’s why it took seven years—five to make the crystals, two to solve the structure.” Analyzing diffraction from 30 crystals, the researchers obtained structures for seven—each with the polyglutamine region in a different conformation.
21 september 2009
Huntingtons dark secret
Scientists have toiled well over a decade trying to determine the structure of huntingtin, one of nine polyglutamine (polyQ)-containing proteins known to cause neurodegenerative disease when misfolded forms of the molecule aggregate in the brain. The current study unveils the first crystal structure of a polyQ-expanded protein (>Q10) in its native context. Seven was the magic number in this technological tour de force. “Because the structure itself is not well formed, it was very difficult to make the crystals, and the x-ray diffraction was very complicated,” Kim told ARF. “That’s why it took seven years—five to make the crystals, two to solve the structure.” Analyzing diffraction from 30 crystals, the researchers obtained structures for seven—each with the polyglutamine region in a different conformation.
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