Figure 1.

Structure-based design of annexin A2−S100A10 inhibitors. (a) The interaction between the helical N-terminal annexin A2 peptide (gray CPK coloring) and a binding pocket of S100A10 (green CPK surface); the side chains, including the N-terminal acetyl group of the annexin peptide involved in intimate contact with the receptor through either hydrophobic or hydrogen-bonding (dashed lines) interactions, are shown as solid sticks and are labeled. (b) The hydrophobic (H1 and H2) and hydrophilic (H3) subsites of the S100A10 binding pocket are colored in cyan, yellow, and magenta, respectively. Predicted binding poses of verified virtual screening hits (gray CPK stick models): (c) 1a, (d) 2a, (e) 3, (f) 4, and (g) 5 (refer Chart 1).