Advances in the molecular mechanism of PGK1 binding to substrates before and after T243 phosphorylation.

Recently, Li Guohui, a researcher at the Dalian Institute of Chemical Physics of the Chinese Academy of Sciences, and Yang Weiwei, a researcher at the Shanghai Institute of Biochemistry and Cell Biology of the Chinese Academy of Sciences, teamed up to explain the effects of phosphorylation of key amino acids in glioma cells on tumor cell growth through molecular dynamics simulation, and the results were published in the journal Molecular Cell as co-authors.
Yang's team found that the amino acid T243 phosphorylation of glycolacid (PGK1) can change the affinity of PGK1 and substrate, thus promoting the activity of THE direction of PGK1 glycoenzyme, as well as promoting the antioxidant enzyme, cell proliferation and tumor growth of glioma cells.
however, the molecular level of T243 phosphorylation is not possible to explain in detail how the T243 phosphorylation process affects the molecular mechanism of PGK1 binding to the substrate.
in order to answer this key scientific question, Li Guohui team and Yang Weiwei team worked closely with the molecular dynamics simulation method to study the molecular mechanism of the combination of PGK1 and substrate before and after T243 phosphorylation, and found that the phosphorylation of T243 affected the side chain orientation of another key amino acid (K216), which in turn affected the key interaction of PGK1 and substrate binding, resulting in significant changes in the phosphoric acid and PG1.
this discovery, the experimental results were verified from the molecular level, and the new strategy of glioma treatment was provided with a detailed theoretical basis.
research work is funded by the National Natural Science Foundation of China and the National Science Fund for Distinguished Young People.
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