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Transcript
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 longrange 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.