Yuvaniyama et al., 2003, Nature Structural Biology

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Yuvaniyama et al., 2003, Nature Structural Biology Insights into antifolate resistance from malarial DHFR-TS structures Protein: Thymidylate Synthase Uniprot ID: P07607 GO: 0004799 thymidylate synthase activity (molecular function) Evidence: IDA Transfers: Submitted transfer annotations to 6 good HHPred hits, using ISS and SEAPHAGES GO_REF Standard Annotation: - Plasmodium falciparium Transfer Annotations: - C. elegans (round worm) - Homo Sapiens - Trichinella spiralis (Trichina worm) Panel B in Figure 2 establishes the activity of Thymidylate Synthase in Plasmodium falciparium dihydrofolate reductase-thymidylate synthase. Figure 2 shows the junction region of alpha helix as a docking element onto the DHFR-TS domain interface. The long-range electrostatic interactions are among the major forces attracting the negatively charged alpha helix of a TS domain to the surface groove lined with positively charged amino acids from the helices of the DHFR domain.