Structural basis of allele variation of human thiopurine-S-methyltransferase.

@article{Wu2007StructuralBO,
  title={Structural basis of allele variation of human thiopurine-S-methyltransferase.},
  author={Hong Kun Wu and John R. Horton and Kevin P. Battaile and Abdellah Allali-Hassani and Fernando Tadeu Bueno Martin and Hong Zeng and Peter Loppnau and Masoud Vedadi and Alexey Bochkarev and Alexander N. Plotnikov and Xiaodong Cheng},
  journal={Proteins},
  year={2007},
  volume={67 1},
  pages={198-208}
}
Human thiopurine S-methyltransferase (TPMT) exhibits considerable person-to-person variation in activity to thiopurine drugs. We have produced an N-terminal truncation of human TPMT protein, crystallized the protein in complex with the methyl donor product S-adenosyl-L-homocysteine, and determined the atomic structure to the resolution of 1.58 and 1.89 A, respectively, for the seleno-methionine incorporated and wild type proteins. The structure of TPMT indicates that the naturally occurring… CONTINUE READING

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