Structural Disorder Provides Increased Adaptability for Vesicle Trafficking Pathways
Figure 4
Interactions between pairs of clathrin-associated adaptor proteins.
Complexes formed between clathrin-associated adaptor proteins are presented, in which one partner interacts with a region predicted to be structurally disordered in the unbound form. On the first three panels, the α2 subunit of mouse Ap-2 is the folded partner interacting with (A) rat epsin-1 (PDB 1KY6), (B) mouse intersectin-1 (PDB 3HS8); and (C) mouse EPS15 (Epidermal growth factor receptor substrate 15, PDB: 1KYF). In panel D, a relatively long disordered segment of human stonin-2 interacts with one folded EF-hand domain of human EPS15 (PDB: 2JXC). In each panel, the structure of the complex is depicted on the left and a domain map for each partner is depicted on the right. The top domain map represents the partner that is binding through the structurally disordered region. In panels A to C, the disordered peptides are represented with sticks (purple) while the folded partner is shown in surface representation (white). In panel D, the long disordered segment of human stonin-2 is shown in cartoon representation. For each protein, the domain maps indicate the names and locations of the known Pfam domains (predicted by the PfamScan method), and are shown in gray segments. Regions predicted to be disordered by IUPred are marked in purple segments; regions present in the PDB structure are marked by stars.