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Figure 2.
Figure 2. Schematic diagram and surface structure of the Abl
SH3–SH2 regulatory region. (a) Richardson diagram of the Abl
SH3–SH2 protein showing the relative positions of the SH3 and
SH2 domains in one molecule. The SH2 domain is at the top of the
figure and the SH3 domain at the bottom. In the SH2 domain the
β strands are shown in red and the α helices in green; in the
SH3 domain the β strands are in yellow. The secondary structure
elements are numbered according to the convention of Eck, et
al. [31] with individual residues identified by their position
within each element or connecting loop; this numbering is used
throughout. (The figure was made with the program MOLSCRIPT
[51].) (b) The molecular surface of the Abl SH3–SH2 structure.
The surface is colored according to the local electrostatic
potential, ranging from blue (the most positive region) to red
(the most negative). The putative phosphotyrosine-binding pocket
and a hydrophobic (pTyr + 3 pocket are indicated. Important
residues for the ligand binding of the SH3 domain are also
indicated. Figure 2. Schematic diagram and surface structure
of the Abl SH3–SH2 regulatory region. (a) Richardson diagram
of the Abl SH3–SH2 protein showing the relative positions of
the SH3 and SH2 domains in one molecule. The SH2 domain is at
the top of the figure and the SH3 domain at the bottom. In the
SH2 domain the β strands are shown in red and the α helices in
green; in the SH3 domain the β strands are in yellow. The
secondary structure elements are numbered according to the
convention of Eck, et al. [[3]31] with individual residues
identified by their position within each element or connecting
loop; this numbering is used throughout. (The figure was made
with the program MOLSCRIPT [[4]51].) (b) The molecular surface
of the Abl SH3–SH2 structure. The surface is colored according
to the local electrostatic potential, ranging from blue (the
most positive region) to red (the most negative). The putative
phosphotyrosine-binding pocket and a hydrophobic (pTyr + 3
pocket are indicated. Important residues for the ligand binding
of the SH3 domain are also indicated. (The figure was made using
the program GRASP [[5]52].)
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