Acta Crystallographica. Section F - Structural Biology and Crystallization Communications
Cryptosporidium hominis is a protozoan parasite that causes acute gastro- intestinal illness. There are no effective therapies for cryptosporidiosis, highlighting the need for new drug-lead discovery. An analysis of the protein ligand interactions in two crystal structures of dihydrofolate reductase- thymidylate synthase DHFR-TS) from C. hominis, determined at 2.8 and 2.87 AÊ resolution, reveals that the interactions of residues Ile29, Thr58 and Cys113 in the active site of C. hominis DHFR provide a possible structural basis for the observed antifolate resistance. A comparison with the structure of human DHFR reveals active-site differences that may be exploited for the design of species-selective inhibitors.
Anderson, Amy C., "Two crystal structures of dihydrofolate reductase-thymidylate synthase from Cryptosporidium hominis reveal protein–ligand interactions including a structural basis for observed antifolate resistance" (2005). Open Dartmouth: Faculty Open Access Scholarship. 421.