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. Author manuscript; available in PMC: 2015 Jul 8.
Published in final edited form as: Structure. 2014 Jun 12;22(7):996–1007. doi: 10.1016/j.str.2014.05.003

Figure 2. Residues in the hPreP Chamber Facilitate Substrate Recognition.

Figure 2

(A) HPreP-N catalytic chamber. (B) Two pockets (L111, F123, F124, and L127; and H896 and R888) explain observed cleavage site preference for P1 or P′1 hydrophobic residues, and scissile bonds 2-5 residues distal from substrate C-termini. (C) Labeled acidic residues are proximal to the active site and can facilitate interaction with basic substrate residues (D) A network of hydrophobic resides in hPreP-N permits capture of hydrophobic residues.