Figure 2.
Figure 2. Structure of Ly49/MHC class I complexes. (a)
Superposition of wild-type (blue) and mutant (red) Ly49C -H-2Kb
complexes in the crystallographic asymmetric unit, indicating
close overall similarity. (b) Electron density in the interface
of the mutant Ly49C -H-2Kb complex. The F[o] - F[c] omit map at
2.9 Å resolution is contoured at 2.5 .
Ly49C residues 239 -243 (red), H-2Kb heavy chain residues 111
-117 (blue) and [2]M
residues 58 -60 (yellow) were excluded from the map calculation.
(c) Ribbon diagram of the mutant Ly49C -H-2Kb complex, in which
the crystallographic Ly49C dimer (red) crosslinks two MHC class
I molecules. (d) Structure of the Ly49A -H-2D^d complex, showing
the asymmetric interaction between the Ly49A dimer (green) and
two MHC class I molecules. The two interaction surfaces, site 1
and site 2, are indicated by the dashed circle and rectangle,
respectively. In c and d, the H-2Kb heavy chain is blue, the
ovalbumin peptide (ball-and-stick representation) is red and
[2]M
is yellow.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Immunol
(2003,
4,
1213-1222)
copyright 2003.
.
Ly49C residues 239 -243 (red), H-2Kb heavy chain residues 111
-117 (blue) and 
[2]M
residues 58 -60 (yellow) were excluded from the map calculation.
(c) Ribbon diagram of the mutant Ly49C -H-2Kb complex, in which
the crystallographic Ly49C dimer (red) crosslinks two MHC class
I molecules. (d) Structure of the Ly49A -H-2D^d complex, showing
the asymmetric interaction between the Ly49A dimer (green) and
two MHC class I molecules. The two interaction surfaces, site 1
and site 2, are indicated by the dashed circle and rectangle,
respectively. In c and d, the H-2Kb heavy chain is blue, the
ovalbumin peptide (ball-and-stick representation) is red and