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Figure 1.
Figure 1. Crystal Structure of SOCS3Δ in Complex with the
gp130(pTyr757) Phosphopeptide
(A) Ribbon diagram of SOCS3Δ
with the bound gp130 phosphopeptide shown in stick
representation. The secondary structural elements for the SH2
domain are labeled; α helices are colored purple, β strands
are colored cyan, and loops are colored gray. Carbon atoms in
the gp130 phosphopeptide are colored yellow, oxygen atoms are
red, nitrogen atoms are blue, and the phosphate atom is black.
The gray spheres represent disordered residues in the BG loop.
The N and C termini for the SH2 domain and the phosphopeptide
are indicated by N and C, respectively, in gray (SOCS3Δ) and
yellow (gp130). The right panel is a view from 90° as
indicated; the EF and BG loops are labeled, and the side chain
of Tyr31 (on edge) of the kinase inhibitory region is shown.
This panel and Figures 2A, 2B, 3B, and 3C were rendered with
PyMOL (http://pymol.sourceforge.net).
(B) Molecular surface
representation of SOCS3Δ colored according to electrostatic
potential (blue, positive [+10 kT]; white, neutral; red,
negative [−10 kT]). Residues of the gp130 phosphopeptide are
labeled relative to pTyr757 (P). The course of the EF loop in
the SH2 domain is shown in gray. This panel was rendered with
GRASP (Nicholls et al., 1991).
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