Backbone and ILVM methyl resonance assignments of human thymidylate synthase in apo and substrate bound forms.

ABSTRACT: Human thymidylate synthase (hTS) is a 72 kDa homodimeric enzyme responsible for the conversion of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP), making it the sole source of de novo dTMP in human cells. As a result, hTS is an attractive anti-cancer therapeutic target. Additionally, hTS is known to possess a number of interesting biophysical features, including adoption of active and inactive conformations, positively cooperative substrate binding, half-the-sites activity, and interacting with its own mRNA. The physical mechanisms underlying these properties, and how they may be leveraged to guide therapeutic development, are yet to be fully explored. Here, as a preface to detailed NMR characterization, we present backbone amide and ILVM methyl resonance assignmen

SUBMITTER: Bonin JP 

PROVIDER: S-EPMC7979492 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature