Crystal structure of microsomal prostaglandin E2 synthase provides insight into diversity in the MAPEG superfamily.

@article{Sjgren2013CrystalSO,
  title={Crystal structure of microsomal prostaglandin E2 synthase provides insight into diversity in the MAPEG superfamily.},
  author={Tove Sj{\"o}gren and Johan Nord and Margareta Ek and Patrik Johansson and Gang Liu and Stefan Geschwindner},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2013},
  volume={110 10},
  pages={3806-11}
}
Prostaglandin E2 (PGE2) is a key mediator in inflammatory response. The main source of inducible PGE2, microsomal PGE2 synthase-1 (mPGES-1), has emerged as an interesting drug target for treatment of pain. To support inhibitor design, we have determined the crystal structure of human mPGES-1 to 1.2 Å resolution. The structure reveals three well-defined active site cavities within the membrane-spanning region in each monomer interface of the trimeric structure. An important determinant of the… CONTINUE READING

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