NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase.

@article{Lee2003NMRSO,
  title={NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase.},
  author={Gui-in Lee and Zhaofeng Ding and John C. Walker and Steven R Van Doren},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 20},
  pages={11261-6}
}
Forkhead-associated (FHA) domains are phosphoprotein-binding modules found in diverse signaling proteins that bind partners phosphorylated on threonine or serine. Kinase-associated protein phosphatase from Arabidopsis employs its FHA domain for negative regulation of receptor-like kinase signaling pathways, which are important in plant development. The solution structure of the free state of kinase-interacting FHA domain (KI-FHA) of kinase-associated protein phosphatase has been determined with… CONTINUE READING

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Structure Fold Des

  • B. Qin, S. S. Lam, K. Lin
  • 1999

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