1. Yuvaniyama et al., 2003, Nature Structural Biology
Insights into antifolate resistance from malarial DHFR-TS structures
Protein: Thymidylate Synthase
Uniprot ID: P07607
GO: 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.