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UCSD study reveals the regulatory mechanism of key enzyme
Date:9/20/2007

Discovery of this enzymes molecular structure may help researchers to design drugs that specifically block the protein kinase activity involved in cancer or cardiac disease.

Scientists didnt really understand how the structure unfolded before now, said Taylor, adding that preventing the subunits from coming apart may be an effective way to inhibit diseases caused when PKA is activated and cant turn itself off. Taylor said the researchers were surprised at how much the structure changed when PKA is turned off. The regulatory subunit opens up and literally wraps itself around the catalytic subunit, thus completely turning the signal off, she said.

Taylor is one of the worlds leading experts on the cAMP-dependent protein kinase, an enzyme that serves as a prototype for the entire protein kinase family. This family of enzymes has more than 500 members that are critical for regulation in all multi-cellular organisms, such as humans.

Taylors work in 1991 (reported in the July 26, 1991 issue of the journal Science) revealed the first-ever molecular structure of the catalytic subunit of a protein kinase, one involved in the action of adrenalin within cells. Understanding its structure was a sort of Rosetta stone for learning the structure of all protein kinases, because they all share certain fundamental characteristics.


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Contact: Debra Kain
ddkain@ucsd.edu
619-543-6163
University of California - San Diego
Source:Eurekalert

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