Figure 4.
Figure 4 Distortion of the ATP-binding site caused by
interdomain rearrangement upon pepJIP1 binding. (A) Structural
comparison between JNK3 (green) and pepJIP1-bound JNK1 (violet)
when the C-terminal domains of the kinases are superimposed. The
conformational differences of the N-terminal domains can be
easily distinguished when the conventional view of kinases is
rotated by 45° along the horizontal axis. The yellow circle
indicates the interaction between the 1
helix and the phosphorylation loop in JNK3, but not existing in
JNK1 complexed with pepJIP1. (B) Comparison of ATP-binding sites
between the JNK1 -pepJIP1 (violet) and JNK3 -AMPPNP (green)
complexes. The AMPPNP bound in JNK3 is shown in a ball-and-stick
model. The residues of JNK3 involved in the hydrogen bonding
with AMPPNP are labeled. The side chains of the residues in the
glycine-rich loop including E75 and A74 of JNK3 are omitted for
clarity because the backbone amide groups only are involved in
the hydrogen bonds with the phosphate groups of AMPPNP. (C) The
structural comparison of the residues crucial for the catalytic
activity between the JNK1 -pepJIP1 (violet) and JNK3 -AMPPNP
(green) complexes. The residues in JNK1 and JNK3 are labeled red
and black, respectively. In (B, C), hydrogen bonds are indicated
by dashed lines.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2004,
23,
2185-2195)
copyright 2004.
1
helix and the phosphorylation loop in JNK3, but not existing in
JNK1 complexed with pepJIP1. (B) Comparison of ATP-binding sites
between the JNK1 -pepJIP1 (violet) and JNK3 -AMPPNP (green)
complexes. The AMPPNP bound in JNK3 is shown in a ball-and-stick
model. The residues of JNK3 involved in the hydrogen bonding
with AMPPNP are labeled. The side chains of the residues in the
glycine-rich loop including E75 and A74 of JNK3 are omitted for
clarity because the backbone amide groups only are involved in
the hydrogen bonds with the phosphate groups of AMPPNP. (C) The
structural comparison of the residues crucial for the catalytic
activity between the JNK1 -pepJIP1 (violet) and JNK3 -AMPPNP
(green) complexes. The residues in JNK1 and JNK3 are labeled red
and black, respectively. In (B, C), hydrogen bonds are indicated
by dashed lines.