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Figure 3.
Figure 3. Mode of Binding of the IRK Activation Loop to the
APS SH2 Domain(A) Stereo view of the interactions between
APS(SH2) and the IRK activation loop. The IRK activation loop is
colored yellow and the APS SH2 protomer to which it binds is
colored green. For clarity, the other APS SH2 protomer is not
shown. Hydrogen bonds/salt bridges are shown with black dashed
lines.(B) Path of the IRK activation loop across the APS SH2
domain surface. A ribbon diagram of the APS SH2 dimer is shown,
with the two protomers colored green and purple. The Cα trace
of the IRK activation loop proximal to pTyr-1158 and pTyr-1162
is colored yellow, with the side chains of the two
phosphotyrosines shown in ball-and-stick representation. The SH2
domains of Src (Waksman et al., 1993) and Grb2 (Rahuel et al.,
1996) with bound peptides were superimposed (core β sheets)
with the green APS SH2 protomer, and the phosphopeptides from
the superposition, PQpYEEI for Src (cyan) and PSp YVNVQN for
Grb2 (orange), are displayed as Cα traces, with the
phosphotyrosines shown in ball-and-stick representation. The N-
and C termini of the phosphopeptides are indicated by “N”
and “C” of the appropriate color. The two disordered
residues between βD and αB in the APS SH2 protomers are
represented by small spheres.
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