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. Author manuscript; available in PMC: 2012 May 25.
Published in final edited form as: J Am Chem Soc. 2011 May 3;133(20):7648–7651. doi: 10.1021/ja2006719

Figure 3.

Figure 3

(a) A hypothetical transition-state structure of PRMT1-catalyzed methylation. The key contact residues were constructed according to the crystal structures of human PRMT1 (PDB file: 1OR8), human PRMT3 (PDB file: 2FYT) and mouse PRMT4 (PDB file: 3B3F). (b) Sequence alignment of human PRMT1, PRMT3 and PRMT4 with the conserved residues highlighted. Y39 and M48 of human PRMT1 are highlighted in red, given their proximity to SAM as shown in Fig. 3a. The two residues were replaced with less-bulky amino acids to adapt SAM analogue cofactors.