My research group is interested in how proteins recognize and bind to each other and how various processes in the cell, in particular within the cytoskeleton, are regulated. Structure determination using X-ray crystallography in order to see and understand the atomic details of proteins and their interactions is our main goal, but complementary biophysical and biochemical methods are being used to characterize the proteins of interest and their complexes.

In particular, we are studying proteins participating in the regulation of actin filament dynamics in parasites, such as the apicomplexan malaria-causing species Plasmodium. Malaria is one of the largest world-wide health threats. Plasmodium use their actin filament cytoskeleton for both motility and host cell recognition and invasion. The cytoskeleton of Apicomplexa displays drastic differences to that of higher eukaryotes and is, therefore, an attractive target for anti-malarial research. We have recently determined the structure of profilin from Plasmodium falciparum [Kursula, I. et al. (2008) Structure, 16: 1638-1648]. This structure reveals striking differences to all other profilins, including the mammalian ones, and serves as a starting point in understanding how actin filament dynamics in these parasites are regulated.

Our current work is focusing on the characterization of the interactions between Plasmodium profilin, actin, and formins, as well as actin depolymerizing factors from these parasites.

Please contact me for further details about possible projects!

Inari Kursula

office: BK324

e-mail: inari.kursula@oulu.fi