On the Importance of Polar Interactions for Complexes Containing Intrinsically Disordered Proteins
Figure 1
Radius of gyration (Rg) of interacting proteins.
(a) Rg as a function of protein length for ID segments that interact with partner molecules (red squares, n = 52) and globular protein of the 3D complex dataset (black triangles, n = 762). 3D complex proteins that are disulfide-rich domains (n = 29) or coiled coils (n = 42) are enclosed in dark blue squares and green circles, respectively. The Rg/N threshold of 0.26 Å is represented by the dotted line. (b) Ribbon structure of the ID segment of p27 (red) that “wraps” around its complex partners cyclin A (grey) and Cdk2 (gold) (p27; PDB: 1JSU chain C, Rg = 21 Å, N = 69). (c) Ribbon structure of one of the 3D complexes, α-chymotrypsin (grey) and eglin c (gold) (bovine α-chymotrypsin; PDB: 1ACB chain E, Rg = 16 Å, N = 241). (d) Ribbon structure of the coiled coil EB1 (EB1; PDB: 1WU9 chain A, Rg = 20 Å, N = 59).