Figure 1.
Figure 1. The crystal structure of sSEMA4D. (a) Schematic of
the homodimer. For one subunit the -propeller
is colored from blue at the N terminus to red at the C terminus;
the extrusion (at top), the PSI and the Ig-like domains (at
bottom) are magenta, pink and coral, respectively. (b) The
sSEMA4D subunit labeled to indicate secondary structure
nomenclature and domains. Disulfide bonds are yellow.
Orientation and color coding are as in a. (c) The top and bottom
surfaces of the -propeller.
Distinctive loops at the top surface are color coded as in a,
and the side chains of key solvent-exposed residues are shown as
ball-and-stick. The orientation is rotated by 90° about the
horizontal relative to that in a. (d) The interaction of 4B-C
loops, which forms the heart of the dimerization interface. The
solvent-accessible surface for one of the subunits is rendered
as a semitransparent surface. Residues are shown as
ball-and-stick with color coding for one subunit as in a. The
orientation is rotated by 90° about the vertical relative to
that in a.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2003,
10,
843-848)
copyright 2003.
-propeller
is colored from blue at the N terminus to red at the C terminus;
the extrusion (at top), the PSI and the Ig-like domains (at
bottom) are magenta, pink and coral, respectively. (b) The
sSEMA4D subunit labeled to indicate secondary structure
nomenclature and domains. Disulfide bonds are yellow.
Orientation and color coding are as in a. (c) The top and bottom
surfaces of the