Figure 3.
Figure 3: Structural analyses of the CED-4a-CED-4b interface and
ATP binding. a, The CED-4a-CED-4b interactions consist of a
primary (orange circle) and a secondary (magenta circle) site.
b, A stereo view of the primary interface of the CED-4 dimer.
Helices 8,
11
and 11b,
from CED-4b, stack against the CARD and /
domains
of CED-4a. c, ATP and magnesium are buried in CED-4. ATP
molecules and magnesium ions are highlighted in yellow and
magenta, respectively. d, A stereo view of ATP coordination in
CED-4. Hydrogen bonds are represented by red dashed lines. ATP
is shown in orange, with nitrogen and oxygen atoms shown in blue
and red, respectively.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2005,
437,
831-837)
copyright 2005.
8,
domains
of CED-4a. c, ATP and magnesium are buried in CED-4. ATP
molecules and magnesium ions are highlighted in yellow and
magenta, respectively. d, A stereo view of ATP coordination in
CED-4. Hydrogen bonds are represented by red dashed lines. ATP
is shown in orange, with nitrogen and oxygen atoms shown in blue
and red, respectively.