Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides.

@article{Zhang2003StructureOT,
  title={Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides.},
  author={Xing Zhang and Xiaodong Cheng},
  journal={Structure},
  year={2003},
  volume={11 5},
  pages={
          509-20
        }
}
PRMT1 is the predominant type I protein arginine methyltransferase in mammals and highly conserved among all eukaryotes. It is essential for early postimplantation development in mouse. Here we describe the crystal structure of rat PRMT1 in complex with the reaction product AdoHcy and a 19 residue substrate peptide containing three arginines. The results reveal a two-domain structure-an AdoMet binding domain and a barrel-like domain-with the active site pocket located between the two domains… CONTINUE READING

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