MANHATTAN, Kan. -- A new biophysical and biochemical study may lead to better understanding of how structural flexibility controls the interaction of a protein that is closely involved with cancer, aging and other chronic diseases -- thereby facilitating future development of better therapeutic strategies, according to a Kansas State University biochemist.
Jianhan Chen, an assistant professor of biochemistry, was one of the researchers on a collaborative project that took a combined computational and experimental approach to understand how protein p21 functions as a versatile regulator of cell division. Their latest findings, "Intrinsic disorder mediates the diverse regulatory functions of the Cdk inhibitor p21," were published in a recent edition of Nature Chemical Biology.
The study used computer simulation to rationalize results from biochemical and biophysical experiments, and provided further insights that would guide future investigations, Chen said. In this case, the focus is human protein p21 and its ability to function as an inhibitor of normal cell growth.
The protein has been shown to be an intrinsically disordered protein. This means it lacks a well-defined three-dimensional structure, characteristics that, until roughly a decade ago, were thought to be necessary for the protein to function.
"For a long time it was believed that proteins must fold to function and it was hard to imagine how an unfolded protein could play a role in crucial cellular areas," Chen said. "What researchers before me found was that by lacking a stable structure, this actually turned out to be really, really important to how these proteins function."
Along with being an intrinsically disordered protein, p21 is a versatile cyclin-dependent kinase, or Cdk, inhibitor -- meaning it adapts to and inhibits a range of Cdk-cyclin complexes that regulate eukaryote cell division. It also has been connected to cancer and aging. For ex
|Contact: Jianhan Chen|
Kansas State University