Article
Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats.
FEBS letters - 21 May 2014
Hasegawa Morio, Toma-Fukai Sachiko, Kim Jun-Dal, Fukamizu Akiyoshi, Shimizu Toshiyuki
Abstract excerpt
Protein arginine methyltransferase 7 (PRMT7) is a member of a family of enzymes that catalyze the transfer of methyl groups from S-adenosyl-l-methionine to nitrogen atoms on arginine residues. Here, we describe the crystal structure of Caenorhabditis elegans PRMT7 in complex with its reaction product S-adenosyl-L-homocysteine. The structural data indicated that PRMT7 harbors two tandem repeated PRMT core domains...
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