This month’s School of Medicine Paper of the Month, “The Structure of Lombricine Kinase: Implications for phosphagen kinase conformational changes,” was published in the Journal of Biological Chemistry. The work is the result of a collaboration between OHSU’s Department of Biochemistry and Molecular Biology’s Olga Kirillova, PhD, Omar Davulcu, PhD, Qing Xie, PhD, Michael Chapman, PhD, and colleagues. The research was partially funded by the first award from the OHSU Emerging Technology Fund.
In this paper, Drs. Kirillova and Davulcu use structural biology to understand the atomic structure of Lombricine Kinase, an enzyme responsible for maintaining energy balance within cells of the body of marine worms. Lombricine Kinase is highly similar to Creatine Kinase, a mammalian enzyme important for buffering the energetic unit of the cell, adenosine triphosphate (ATP). An understanding of the molecular structure of this enzyme is critical to understanding the functional role of the enzyme in normal biological processes and disease.
Dr. Chapman hopes that their insight might contribute to a broader understanding of multiple biological enzymes. “This system offers a window on how one might predict many other proteins to behave,” he said.
Read the full article on the School of Medicine website.