Figure 4.
Figure 4. Dronc and Hid compete with each other for binding to
the same surface groove on the BIR2 domain of DIAP1. (a)
Stereo superposition of the structures of DIAP1-BIR2 bound to
Dronc and to Hid peptide. The Dronc and Hid peptides are green
and orange, respectively. Note the difference in the orientation
of the two peptides. Phe118 of Dronc and Phe4 of Hid occupy the
same general pocket on the surface of DIAP1. (b) A ten-residue
peptide derived from the N terminus of Hid disrupts the
interaction between Dronc and DIAP1. GST-BIR2-Dronc (1 -136)
complex (1.2 mg) was used for each gel filtration run. Hid
peptide (60 g)
was used to disrupt the BIR2 -Dronc complex. The chromatograms
for gel filtration are on the left and the relevant fractions
from gel filtration were visualized by SDS-PAGE and stained with
Coomassie blue.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2003,
10,
892-898)
copyright 2003.
g)
was used to disrupt the BIR2 -Dronc complex. The chromatograms
for gel filtration are on the left and the relevant fractions
from gel filtration were visualized by SDS-PAGE and stained with
Coomassie blue.