Figure 1.
Figure 1: Mapping the binding sites on the Vti1b H[abc] domain
and the EPNR ENTH Delta-alpha-0
domain on their isolated structures. a, b, Ribbon diagram
showing the three-helix bundle (H[abc] domain) of uncomplexed
Vti1b (a, light green) and of uncomplexed EPNR ENTH 0
(b, pale pink). Surface views are shown in the same
orientations. Mutated residues on both representations are
coloured green if they affected binding to EPNR, pink if they
affected binding to Vti1b H[abc] and grey-blue if there was no
effect (surface views only). c–f, Pull-down experiments
detecting the binding of EPNR ENTH–Myc constructs to
GST–Vti1b by western blotting for the Myc tag. c, The effect
of mutations in GST–Vti1b on their binding of wild-type EPNR
ENTH–Myc. d, e, The effect of point (d) and helix-deletion (e)
mutations in EPNR ENTH–Myc on their binding to wild-type
GST–Vti1b. f, The effect of the charge-swap mutations
EPNR(R146E) and Vti1b(E23R) introduced on the basis of the
complex structure.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2007,
450,
570-574)
copyright 2007.
alpha-
0
domain on their isolated structures. a, b, Ribbon diagram
showing the three-helix bundle (H[abc] domain) of uncomplexed
Vti1b (a, light green) and of uncomplexed EPNR ENTH 
0
(b, pale pink). Surface views are shown in the same
orientations. Mutated residues on both representations are
coloured green if they affected binding to EPNR, pink if they
affected binding to Vti1b H[abc] and grey-blue if there was no
effect (surface views only). c–f, Pull-down experiments
detecting the binding of EPNR ENTH–Myc constructs to
GST–Vti1b by western blotting for the Myc tag. c, The effect
of mutations in GST–Vti1b on their binding of wild-type EPNR
ENTH–Myc. d, e, The effect of point (d) and helix-deletion (e)
mutations in EPNR ENTH–Myc on their binding to wild-type
GST–Vti1b. f, The effect of the charge-swap mutations
EPNR(R146E) and Vti1b(E23R) introduced on the basis of the
complex structure.