An isolated, purified, and tested rat protein arginine methyltransferase, type 1 (PRMT1) His- S11-R361.
- Structures of PRMT1-AdoHyc and its complex with peptide substrates.
- Have active site residues and peptide binding channels.
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.
Protein available for licensing.
Publication: Zhang & Cheng. Structure, 2003. 11:509-520.