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. 2020 Feb 27;477(4):787–800. doi: 10.1042/BCJ20190826

Figure 5. Sequence conservation of CARM1-N265 across other PRMTs and position of substrate arginine-interacting glutamic acid residue in PRMT structures.

Figure 5.

(A) Sequence alignment of human PRMT active sites showing site of N265Y mutation generated using ClustalW and Box Shade. The site targeted for mutagenesis is highlighted in yellow. Sites that show >50% consensus are shaded (black for identical residues and grey for similar residues). Colour coding matches the structures shown in (B). (B) Superposition of PRMT1 (1OR8, hot pink [50]), PRMT2 (5JMQ, yellow), PRMT3 (1F3L, green [51]) and PRMT8 (5DST, blue [52]) with CARM1 (WT) (bound to 9, light grey, all monomers in the asymmetric unit shown) and CARM1-N265Y (bound to 10, teal), which all have a tyrosine or phenylalanine adjacent to the active site glutamate.