Figure 2.
Figure 2: Fc alpha-structure.
a, Ribbon diagrams showing front (left) and side (right)
views of Fc (top)
and Fc (bottom)33.
Disulphide bonds are shown in yellow and carbohydrate residues
are shown in ball-and-stick representation. b, Topology diagram
of Fc .
-Strands
are blue or magenta, 3[10] and -helices
are light blue and disulphides are yellow. The proposed C241
-C241 disulphide bond (not present in our construct) is shown as
a dashed yellow line. Blue and magenta dots show residues that
contact Fc RI.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2003,
423,
614-620)
copyright 2003.
structure.
a, Ribbon diagrams showing front (left) and side (right)
views of Fc 
(top)
and Fc 
(bottom)33.
Disulphide bonds are shown in yellow and carbohydrate residues
are shown in ball-and-stick representation. b, Topology diagram
of Fc 
-Strands
are blue or magenta, 3[10] and