Figure 2.
Figure 2 Overall view of IRK3P and comparison with IRK. (A)
Ribbon diagram of the IRK3P structure. The -helices
are shown in red, the -strands
in blue, the nucleotide-binding loop in yellow, the catalytic
loop in orange, the activation loop in green, AMP-PNP in black
and the peptide substrate in pink. The termini are denoted by N
and C. (B) Superposition of the C-terminal lobes of IRK and
IRK3P. The backbone representation of IRK/IRK3P is colored
orange/green, with the activation loop colored red/blue. The
axis (black) and arrow (blue) specify the rotation required to
align the N-terminal -sheet
of IRK with that of IRK3P. (C) Superposition of the -sheets
in the N-terminal lobes of IRK and IRK3P. The backbone
representation and carbon atoms of IRK/IRK3P are colored
orange/green, oxygen atoms are red and nitrogen atoms are blue.
(A) and (C) prepared with RIBBONS (Carson, 1991), (B) with GRASP
(Nicholls et al., 1991).
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(1997,
16,
5572-5581)
copyright 1997.
-helices
are shown in red, the 
-strands
in blue, the nucleotide-binding loop in yellow, the catalytic
loop in orange, the activation loop in green, AMP-PNP in black
and the peptide substrate in pink. The termini are denoted by N
and C. (B) Superposition of the C-terminal lobes of IRK and
IRK3P. The backbone representation of IRK/IRK3P is colored
orange/green, with the activation loop colored red/blue. The
axis (black) and arrow (blue) specify the rotation required to
align the N-terminal