Figure 3.

Cellular clathrin‐box motifs (CBMs) bind in a different conformation than arrestin2L at the arrestin box. A, The surface of clathrin N‐terminal domain (NTD) is shown (grey) oriented as in Figure 2 (left) and rotated by 90° around the horizontal axis (right). The AmphCBM_pep peptide bound at the arrestin box is shown as coloured spheres. B, Close‐up view of cellular CBM‐containing peptides bound at the arrestin box. Peptides are shown as sticks coloured as in Figure 2. The surface of clathrin NTD is shown, coloured from high (green) to low (white) surface residue hydrophobicity, with outlines of selected surface side chains shown in grey. Bound AP2CBM_pep residues are numbered by their position in the LΦxΦ[DE] CBM consensus sequence. C, The extended surface loop of arrestin 2 long isoform (arrestin2L) bound at the arrestin box (PDB 3GD1).13 NTD is shown as in (B) and arrestin2L residues 332‐340 are shown as sticks with cyan carbon atoms. Note that in (B) the direction of the bound peptides is right (N terminus) to left (C terminus), whereas in (C) the peptide chain between residues L334‐L338 runs in the opposite direction.