Technology Listings

Protein Arginine Methyltransferase 1 (PRMT1) His- S11-R361


An isolated, purified, and tested rat protein arginine methyltransferase, type 1 (PRMT1) His- S11-R361.

Key Benefits
  • Structures of PRMT1-AdoHyc and its complex with peptide substrates.
  • Have active site residues and peptide binding channels.
Technical Summary

Protein arginine methylation is a common posttranslational modification in eukaryotes. The major type of PRMT1 transfers the methyl group from S-adenosyl-L-methionine (AdoMet) to the guanidine group of arginines in protein substrates. The rat PRMT1 described here is in complex with the reaction product S-adenosyl-L-homocysteine (AdoHcy) and with peptide substrates. The protein has a two-domain structure with the active site pocket located between the two domains. The two active site glutamates are essential for enzymatic activity and dimerization of PRMT1 is essential for AdoMet binding. In addition, three peptide binding channel have been identified by the researchers.

Developmental Stage

Protein available for licensing.

Publication: Zhang & Cheng. Structure, 2003. 11:509-520.

Patent Information
Tech ID: 07144
Published: 6/7/2013
Research Tools

Rajsekhar Guddneppanavar
Licensing Associate
Emory University

Xiaodong Cheng
Xing Zhang