Figure 2.
Figure 2: Crystal structure of SAP–Fc bold gamma-RIIa
complex. a–c, The view is from the face (a) and sides (b,
c) of SAP; in c only the receptor contact A and C subunits are
highlighted. The five SAP subunits are shown in yellow with
ridge helices in red, and Fc RIIa
is coloured blue. The interface is represented by a molecular
surface in green. The Ca^2+-binding and ligand-binding sites on
SAP are highlighted in magenta. d, Comparison between the free
(green) and receptor-bound (yellow) SAP, and between the free
(wheat) and SAP-bound (blue) Fc RIIa
structures. For clarity, only the A subunit is shown from the
superposition of SAP pentamer. The BC loop (residues 28–35) of
the D1 domain is indicated.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
Nature
(2008,
456,
989-992)
copyright 2008.
RIIa
complex. a–c, The view is from the face (a) and sides (b,
c) of SAP; in c only the receptor contact A and C subunits are
highlighted. The five SAP subunits are shown in yellow with
ridge helices in red, and Fc 
RIIa
is coloured blue. The interface is represented by a molecular
surface in green. The Ca^2+-binding and ligand-binding sites on
SAP are highlighted in magenta. d, Comparison between the free
(green) and receptor-bound (yellow) SAP, and between the free
(wheat) and SAP-bound (blue) Fc