| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5917357 | Molecular Immunology | 2013 | 7 Pages |
Abstract
⺠The crystal structure of the IgG4 CH3 domain dimer has been solved at 1.8 Ã
resolution. ⺠The effect of Arg409 on the IgG4 CH3 interface is revealed by comparison with IgG1. ⺠Arg409 disrupts a network of water molecules that is conserved in IgG1. ⺠Arg409 weakens the interaction at the CH3 interface. ⺠The mechanism by which Arg409 predisposes human IgG4 to Fab-arm exchange is proposed.
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Authors
Anna M. Davies, Theo Rispens, Tamara H. den Bleker, James M. McDonnell, Hannah J. Gould, Rob C. Aalberse, Brian J. Sutton,