Sergey Korolev, Ph.D., Associate Professor of Biochemistry, published findings in Nature Communications revealing the crystal structure of the calcium-independent form of phospholipase A2β (iPLA2β). The structure sheds new light on the function, cellular localization, and regulation of this enzyme.

Calcium-independent iPLA2β plays a role in regulation of inflammation, calcium homeostasis, and apoptosis, as well as some neurodegenerative diseases, such as Parkinson’s disease. Discovering the crystal structure of the enzyme reveals locations of the catalytic domains and active sites, which could lead to development of therapeutic small molecules for treatment of disease-associated mutations.

Also pictured are Ian Miller (left), Research Assistant in the Korolev lab, and Konstantin Malley, Ph.D. (middle). Dr. Malley is a former graduate student in the department and is first author on the publication. He is in the M.D./Ph.D. program at SLU and is currently pursuing his M.D. degree.

For more information, read the full article in Newslink.