1sej

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Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase from Cryptosporidium hominis Bound to 1843U89/NADPH/dUMP

Overview

Cryptosporidium hominis is a protozoan parasite that causes acute, gastrointestinal 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 A 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.

About this Structure

1SEJ is a Single protein structure of sequence from Cryptosporidium hominis with UMP, F89 and NDP as ligands. Full crystallographic information is available from OCA.

Reference

Two crystal structures of dihydrofolate reductase-thymidylate synthase from Cryptosporidium hominis reveal protein-ligand interactions including a structural basis for observed antifolate resistance., Anderson AC, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 Mar 1;61(Pt, 3):258-62. Epub 2005 Feb 8. PMID:16511011

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