Sergey Korolev, Ph.D., 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.
Konstantin Malley, Ph.D., a former graduate student in the department, is first author on the publication. Dr. Malley is in the M.D./Ph.D. program at SLU and is currently pursuing his M.D. degree.
Sequence motifs and the structure of iPLA2β.