N-terminal specificity of decapeptide trimming by ERAP1.

<p>All peptides are based on the same template varying in their N-terminus (indicated as X in the sequence below the graph). 100 µM of each peptide was incubated with 40 ng of ERAP1 at 37°C and the reaction products analyzed as in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0003658#pone-0003658-g001" target="_blank">figure 1</a>. A representative experiment is shown here. Peptides carrying hydrophobic residues at their N-termini were trimmed fastest, whereas peptides carrying charged (R, K or E) or hydrophilic (T) residues in their N-termini were more resistant to cleavage by ERAP1.