Figure 2 - full size

 

Figure 2.
FIGURE 2. Interactions between the Rituximab Fab and the epitope peptide. A, an overview showing the interactions of the epitope peptide with the Rituximab Fab. The Fab CDRs are shown with the H1 loop in orange, H2 in green, H3 in tinted green, L1 in gold, L2 in pink, and L3 in purple. The peptide is colored in cyan. The four CDR loops (H1, H2, H3, and L3) of the Fab form a pocket to accommodate the epitope peptide. B, an electrostatic potential surface of the Rituximab Fab in the region of the epitope peptide binding pocket showing the structural and chemical complementarity between the Fab and the bound peptide. The residues of the epitope peptide involved in interactions with the Fab are shown with ball and stick models. The ^170ANPS^173 motif of the CD20 epitope is located in a pocket formed by CDR loops H1, H2, H3, and L3 of the Fab. The locations of a few residues of the Fab are labeled for reference. C, a stereoview showing the hydrogen-bonding interactions between residues of the epitope peptide and CDR loops H1 and H3 of the Fab. The color coding of the structural elements is the same as A. D, a stereoview showing the hydrogen bonding between the epitope peptide and CDR loops H2 and L3 of the Fab.

The above figure is reprinted by permission from the ASBMB: J Biol Chem (2007, 282, 15073-15080) copyright 2007.