Structural basis of polyethylene glycol recognition by antibody.
Cheng-Chung LeeYu-Cheng SuTzu-Ping KoLi-Ling LinChih-Ya YangStanley Shi-Chung ChangSteve R RofflerAndrew H-J WangPublished in: Journal of biomedical science (2020)
The differing amino acids in 3.3 and 2B5 are not involved in PEG binding but engaged in dimer formation. In particular, the light-chain residue K53 of 2B5-Fab makes significant contacts with the other Fab in a dimer, whereas the corresponding N53 of 3.3-Fab does not. This difference in the protein-protein interaction between two Fab molecules in a dimer may explain the temperature dependence of 2B5 in PEG binding, as well as its inhibition by crown ether.