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Novel strategies targeting bifunctional TS-DHFR in parasitic infections
Dr. Karen Anderson from Yale University, presents this seminar.
About Dr. Anderson
Karen S. Anderson is a Professor of Pharmacology and Molecular Biophysics and Biochemistry. She is involved in teaching undergraduates and graduate students about drug discovery and structure-based drug design. Dr. Anderson's research utilizes mechanistic enzymology and structure-based drug design. Her work focuses on understanding how enzymes, playing critical roles in such diseases as cancer and infectious diseases, including AIDS, work at a molecular level. She uses that information to develop new drug therapies. She has trained over 50 students and postdocs who have gone on to graduate - and medical schools as well as and successful careers in academia and industry.
About the Seminar
Thymidylate synthase (TS) and dihydrofolate reductase (DHFR) are critical enzymes for DNA biosynthesis. In contrast to human monofunctional forms of thymidylate synthase (TS) and dihydrofolate reductase (DHFR), protozoal parasites like Cryptosporidium and Toxoplasma and other protozoal species encode TS and the DHFR on a single polypeptide chain, with DHFR N-terminal to TS. It has been suggested that these bifunctional TS-DHFR enzymes may used substrate channeling as a mechanism for more efficient transfer of dihydrofolate from TS to DHFR site. Mechanistic and structural studies have revealed new insights into these processes that suggest new strategies to exploit for design of new antiparasitic drugs.