Ontology highlight
ABSTRACT:
SUBMITTER: Ishino T
PROVIDER: S-EPMC3675588 | biostudies-literature | 2013 Jun
REPOSITORIES: biostudies-literature
Ishino Tetsuya T Wang Mengmeng M Mosyak Lidia L Tam Amy A Duan Weili W Svenson Kristine K Joyce Alison A O'Hara Denise M DM Lin Laura L Somers William S WS Kriz Ronald R
The Journal of biological chemistry 20130424 23
Human IgG is a bivalent molecule that has two identical Fab domains connected by a dimeric Fc domain. For therapeutic purposes, however, the bivalency of IgG and Fc fusion proteins could cause undesired properties. We therefore engineered the conversion of the natural dimeric Fc domain to a highly soluble monomer by introducing two Asn-linked glycans onto the hydrophobic C(H)3-C(H)3 dimer interface. The monomeric Fc (monoFc) maintained the binding affinity for neonatal Fc receptor (FcRn) in a pH ...[more]