Figure 2
AHNAK binds to various pockets on the surface of the S100A10-AnxA2 tetramer. The binding of AnxA2 to S100A10 increases the surface area of the largely hydrophobic surface formed across the dimeric interface of helix IV of S100A10 chains A and B by 363 Å2, allowing more interactions with AHNAK (yellow sticks). Removal of AnxA2 leaves the N- and C-terminal portions of AHNAK without a binding surface (upper right inset). Several hydrophobic residues of AHNAK insert themselves into hydrophobic pockets on the surface of S100A10-AnxA2, while the side chains of polar and charged residues mainly point towards the solvent (lower insets). The surface of S100A10-AnxA2 is colored by electrostatic potential, with red representing electronegative regions and blue representing electropositive regions.  [article HTML]

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