Figure 1.
FIGURE 1. Overall structure of the Rituximab Fab-CD20
epitope-peptide complex. A, overall structure of the complex.
The Rituximab Fab is colored with the light chain in yellow and
the heavy chain in green, and the CD20 epitope peptide in cyan.
B, a stereoview of a composite-omit electron density map at
2.6-Å resolution for the bound epitope peptide contoured
at 1.0- level. The atomic
coordinates of the peptide residues are shown in ball and stick
models. C, structure of the bound epitope peptide. The epitope
peptide consists of a short N-terminal coil (residues 167-171),
a 3[10] helix (residues 172-174), a small loop (residues
175-177), and a short C-terminal -helix (residues
178-184). The intra-peptide hydrogen-bonding interactions
between residues of the middle part (the 3[10] helix and the
small loop) and the other parts of the peptide are indicated
with dashed lines.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2007,
282,
15073-15080)
copyright 2007.
level. The atomic
coordinates of the peptide residues are shown in ball and stick
models. C, structure of the bound epitope peptide. The epitope
peptide consists of a short N-terminal coil (residues 167-171),
a 3[10] helix (residues 172-174), a small loop (residues
175-177), and a short C-terminal 
-helix (residues
178-184). The intra-peptide hydrogen-bonding interactions
between residues of the middle part (the 3[10] helix and the
small loop) and the other parts of the peptide are indicated
with dashed lines.