p16INK4, which is a 16-kDa polypeptide protein, inhibits the catalytic activity of the CDK4-cyclinD complex to suppress tumor growth. Both unlabeled and isotopelabeled human tumor suppressor p16INK4 protein were overexpressed and purified to characterize biochemical and structural properties. The purified p16 binds to monomeric GST-CDK4 and exists in a monomer conformation for several weeks at 4°C. The circular dichroism (CD) data indicates that p16 contains high percentage of α-helix and that the helix percentage maximized at pH value of 7.0. One- and two-dimensional nuclear magnetic resonance (NMR) data suggest that purified p16 from our construct has a unique folded conformation under our experimental conditions and exhibits quite stable conformational characteristics.
|Number of pages||5|
|Journal||Journal of Biochemistry and Molecular Biology|
|Publication status||Published - 1998 Jan 31|
All Science Journal Classification (ASJC) codes
- Molecular Biology