Figure 5.

Comparison of AHNAK C-terminal peptides that display a range of binding affinities to the S100A10–AnxA2 tetramer. The 20-mer AHNAK peptide used in the cocrystallization experiment is highlighted in yellow. Phe5 and Phe13, both of which have strong electron density for their side chains, are shown in bold along with corresponding residues in the other peptides. Sequences colored in green show the tightest binding in previous studies, while those in red showed weak binding (Rezvanpour et al., 2011 ▶). The original consensus sequence (1) is listed below the peptide sequences and a revised consensus sequence (2; outlined) based on the crystal structure is also included. ϕ, hydrophobic; +, positively charged; X, variable; Z, charged/polar.