Schuck P, Radu C G, Ward E S
Molecular Interactions Resource ORS, Bioengineering and Physical Science Program, National Institutes of Health, Bethesda, MD 20892-5766, USA.
Mol Immunol. 1999 Oct-Nov;36(15-16):1117-25. doi: 10.1016/s0161-5890(99)00093-0.
The interaction of mouse IgG1 or IgG1-derived Fc fragment with recombinant, insect cell expressed mouse FcRn has been analyzed using sedimentation equilibrium. This results in a model for the interaction in which the two binding sites for FcRn on Fc or IgG1 have significantly different affinities with macroscopic binding constants of < 130 nM and 6 microM. This data indicates the formation of an asymmetric FcRn:Fc (or IgG1):FcRn complex which is consistent with earlier suggestions that for this form of recombinant FcRn, binding to IgG1 or Fc does not result in a symmetric 2:1 complex in which both binding sites are equivalent.