Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53.

@article{Liao1999StructureAF,
  title={Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53.},
  author={H Liao and In Ja L Byeon and Ming Daw Tsai},
  journal={Journal of molecular biology},
  year={1999},
  volume={294 4},
  pages={1041-9}
}
The forkhead-associated (FHA) domain is a 55-75 amino acid residue module found in >20 proteins from yeast to human. It has been suggested to participate in signal transduction pathways, perhaps via protein-protein interactions involving recognition of phosphopeptides. Neither the structure nor the ligand of FHA is known. Yeast Rad53, a checkpoint protein involved in DNA damage response, contains two FHA domains, FHA1 (residues 66-116) and FHA2 (residues 601-664), the second of which recognizes… CONTINUE READING
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PROCHECK: a program to check the stereochemical quality of protein structures

  • R. A. Laskowski, M. W. MacArthur, D. S. Moss, J. M. Thornton
  • J. Appl. Crystallog
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