EC Number   |
Reference |
|---|
   2.1.1.320 | - |
756415 |
| 2.1.1.320 | complex of isoform PRMT5, methylosome protein MEP50 and S-adenosylhomocysteine. PRMT5-MEP50 forms an unusual tetramer of heterodimers with substantial surface negative charge. MEP50 is required for PRMT5-catalyzed histone H2A and H4 methyltransferase activity and binds substrates independently. MEP50 binds to the substrate distal of the target arginine and orients the unstructured substrate tail towards the catalytic site of the PRMT5 molecule that is not directly coupled to the substrate-bound MEP50 |
735085 |
| 2.1.1.320 | crystal structure of isoform PRMT5 in complex with methylosome protein MEP50, bound to an S-adenosylmethionine analog and a peptide substrate derived from histone H4 |
735162 |
| 2.1.1.320 | in a structural model, the carboxylate group of the position 4 Asp258 points away from the substrate arginine, possibly to coordinate the binding of one or both of the two lysine residues adjacent to the methylated arginine in the FKRKY sequence of substrate SF3B2 |
734308 |
