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Structure of enzyme offers treatment clues for diabetes, Alzheimer's

sions of wide-open IDE proved to be 30 to 40 times more active than the normal version of the enzyme.

"This suggests that the rate-limiting step may be the speed at which the enzyme can reopen and then clamp down on a new morsel rather than the time it takes to chew something up," said Tang. "This makes us think that if we can slightly alter its shape, we can substantially boost its activity."

The researchers are now searching for small molecules that can duplicate the effects of those mutations, shifting the balance toward the open rather than the closed state. "Such compounds," the authors note, "might facilitate the clearance of amyloid-beta and other pathologically relevant IDE substrates."

"By revealing IDE's active site in unprecedented detail," notes the commentary, "the new structures provided by Tang and coworkers hold great promise for finally realizing Mirsky's dream."


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Contact: John Easton
John.Easton@uchospitals.edu
773-702-6241
University of Chicago Medical Center
11-Oct-2006


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