Article
Structures of human thymidylate synthase R163K with dUMP, FdUMP and glutathione show asymmetric ligand binding.
Acta crystallographica. Section D, Biological crystallography - 1 Jan 2011
Gibson Lydia M, Celeste Lesa R, Lovelace Leslie L, Lebioda Lukasz
Abstract excerpt
Thymidylate synthase (TS) is a well validated target in cancer chemotherapy. Here, a new crystal form of the R163K variant of human TS (hTS) with five subunits per asymmetric part of the unit cell, all with loop 181-197 in the active conformation, is reported. This form allows binding studies by soaking crystals in artificial mother liquors containing ligands that bind in the active site. Using this approach,...
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