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Figure 1.
(a) Domain architecture of Grb7, Grb10 and Grb14 drawn to
linear scale (human Grb10, isoform c, 536 residues). P,
proline-rich region; RA, Ras-associating domain; PH,
pleckstrin-homology domain; BPS, between PH and SH2 region; SH2,
Src-homology-2 domain. (b) Ribbon diagram of the crystal
structure of Grb10 RA-PH. One copy of RA-PH is colored violet
(RA) and cyan (PH), and the second copy is colored orange (RA)
and green (PH). For both copies, the RA-PH linker is gray. The
binding sites for small GTPases on the RA domain and
phosphoinositides on the PH domain (noncanonically) are
indicated by the position of the labels 'RA' and 'PH'. An
approximate twofold axis (vertical, in the plane of the figure)
relates the two molecules in the asymmetric unit. Select
secondary-structure elements are labeled, as are the N and C
termini. Right, the structure has been rotated 90°, as
indicated, with the molecular twofold axis perpendicular to the
plane of the figure. (c) Stereo view of the dimerization
interface. The view is the same as in the right panel of b. Side
chains that mediate the interaction between the two RA-PH
molecules are shown in stick representation. Hydrogen bonds and
salt bridges are represented by black dashed lines, and the side
chains of hydrophobic residues are shown with a van der Waals
surface. (d) Stereo view of the interface between the RA and PH
domains. Pictorial conventions as in c. Figures 1,3c,d and 6
were rendered with PyMol (http://pymol.sourceforge.net).
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