Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution.

@article{Reinemer1992ThreedimensionalSO,
  title={Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution.},
  author={Peter Reinemer and Heini W Dirr and Rudolf Ladenstein and Robert Huber and Mario Lo Bello and Giorgio Federici and Michael W. Parker},
  journal={Journal of molecular biology},
  year={1992},
  volume={227 1},
  pages={
          214-26
        }
}
The three-dimensional structure of human class pi glutathione S-transferase from placenta (hGSTP1-1), a homodimeric enzyme, has been solved by Patterson search methods and refined at 2.8 A resolution to a final crystallographic R-factor of 19.6% (8.0 to 2.8 A resolution). Subunit folding topology, subunit overall structure and subunit association closely resembles the structure of porcine class pi glutathione S-transferase. The binding site of a competitive inhibitor, S-hexylglutathione, is… CONTINUE READING

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