Figure 2.
Figure 2: The EPNR ENTH Delta-alpha-0–Vti1b
H[abc] domain complex. a, The complex is shown, with Vti1b
coloured dark green to pale green (N to C) and EPNR coloured
pale pink to dark pink (N to C). Enlarged views are shown of key
residues in the binding interface. The putative lipid binding
helix 0
of EPNR is shown in grey. The proposed orientation of the
remaining portions of Vti1b and EPNR are indicated by dotted
lines. Charge-swap mutations are boxed. b, Surface
representations of the complex, with each rotated by 90 degrees
to show the 'footprint' of interaction coloured green on Vti1b
H[abc] and pink on EPNR ENTH. C ribbons
and side chains participating in the interaction are shown
through the different surfaces. Mutated residues that have been
demonstrated to affect binding are boxed. c, Structure-based
sequence alignment of the H[abc] domains of mouse Vti1b, mouse
Vti1a and yeast Vti1 (with conserved residues boxed in green),
and of human EPNR ENTH domain with yeast Ent3 (with conserved
residues shown in pink). Residues in which mutation abolishes
binding between Vti1b and EPNR are marked with an asterisk.
Residues that have significant roles in the binding interface
are indicated by a triangle.
alpha-
0–Vti1b
H[abc] domain complex. a, The complex is shown, with Vti1b
coloured dark green to pale green (N to C) and EPNR coloured
pale pink to dark pink (N to C). Enlarged views are shown of key
residues in the binding interface. The putative lipid binding
helix 
0
of EPNR is shown in grey. The proposed orientation of the
remaining portions of Vti1b and EPNR are indicated by dotted
lines. Charge-swap mutations are boxed. b, Surface
representations of the complex, with each rotated by 90 degrees
to show the 'footprint' of interaction coloured green on Vti1b
H[abc] and pink on EPNR ENTH. C