Structure of the catalytic domain of Plasmodium falciparum ARF GTPase-activating protein (ARFGAP)

Acta Cryst. (2011). F67, 1339-1344 (http://doi.org/g3k)

Two molecules of ARFGAP related by the noncrystallographic twofold axis form a dimer in the asymmetric unit. A number of residues on this interface are distinct in the P. falciparum ARFGAP.

ADP ribosylation factor GTPase-activating proteins (ARFGAPs) play multiple roles in cellular signal transduction and protein trafficking, which are necessary for the survival and growth of the Plasmodium falciparum parasite. A strategy for interrupting the protein-trafficking machinery within plasmodium-infected erythrocytes may be effective in arresting the life cycle of the parasite and thereby preventing disease progression. The structure of the catalytic domain of the Plasmodium ARFGAP shows several notable differences from human ARFGAP; these unique properties may offer new targets for therapeutic intervention.