Article
Profiling substrates of protein arginine N-methyltransferase 3 with S-adenosyl-L-methionine analogues.
ACS chemical biology - 21 Feb 2014
Guo Han, Wang Rui, Zheng Weihong, Chen Yuling, Blum Gil, Deng Haiteng, Luo Minkui
Abstract excerpt
Protein arginine N-methyltransferase 3 (PRMT3) belongs to the family of type I PRMTs and harbors the activity to use S-adenosyl-l-methionine (SAM) as a methyl-donor cofactor for protein arginine labeling. However, PRMT3's functions remain elusive with the lacked knowledge of its target scope in cellular settings. Inspired by the emerging Bioorthogonal Profiling of Protein Methylation (BPPM) using engineered...
Topics
- Amino Acid Sequence
- Binding Sites
- Humans
- Methylation
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis
- Mutation
- Protein-Arginine N-Methyltransferases
- S-Adenosylmethionine
- Sequence Alignment
- Substrate Specificity