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. Author manuscript; available in PMC: 2009 Aug 27.
Published in final edited form as: Annu Rev Biophys Biomol Struct. 2005;34:267–294. doi: 10.1146/annurev.biophys.34.040204.144452

Figure 8.

Figure 8

Peptide-binding grooves (P1, P2, and P3) in the structure of ternary complex of PRMT1-AdoHcy-R3 peptide (sequence shown at the bottom): solvent-accessible molecular surface with bound AdoHcy and arginine shown as stick models and indicated by the arrows (left panel). If the central Arg-9 were the target bound in the active site, connecting peptide-binding sites P1 and P2 would cover the active site and the entire length of the peptide. When the end arginine (either Arg-3 or Arg-15) is bound in the active site, connection of peptide-binding sites P2 and P3 would account for the length of the whole peptide (right panel). Site P3 corresponds to one of the grooves perpendicular to the strands of the β-barrel domain.