|
Figure 3.
Figure 3. Positions that Affect Affinity for Human FcRn
Highlighted on the Structure of Human FcA single polypeptide
chain from the structure of human Fc (coordinates obtained from
Mark Ultsch, Genentech) is shown with side chains highlighting
positions where substitutions result in reduced (red side chain)
or enhanced (green side chain) affinity for human FcRn, based
upon mutagenesis studies by Shields et al. (2001) (Table 4).
Residues within the predicted interface with human FcRn (within
5 Å of an FcRn atom using a human FcRn/human Fc model
generated from the rat FcRn/hdFc structure) are indicated by
thick side chains and labels. Residues predicted to be outside
of the interface are indicated by thin side chains and smaller
labels
|