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The overexpression of the M2 isoform in tumor cells invokes many mechanistic questions regarding the role of hPKM2 in tumorgenesis, as well as offers an intriguing anti-cancer target. Therefore, our structure may be useful as a template for the discovery of novel compounds that may serve as possible anti-cancer drug leads. We cloned, overexpressed, and purified hPKM2 from inclusion bodies in E. coli through a unique refolding protocol. The enzyme was crystallized and x-ray data were collected at the APS (Argonne National Labs). The human PKM2 crystal structure was determined to 2.8 Å resolution. Structural analysis and comparison of structural differences among isozymes is presented here.