Substitution at Residue 214 of Human Thymidylate Synthase Alters Nucleotide Binding and Isomerization of Ligand−Protein Complexes
Based on crystal structures of bacterial thymidylate synthases (TS), a glutamine corresponding to residue 214 in human TS (hTS) is located in a region that is postulated to be critical for conformational changes that occur upon ligand binding. Previous steady-state kinetic studies indicated that rep...
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Veröffentlicht in: | Biochemistry (Easton) 1999-04, Vol.38 (17), p.5582-5587 |
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