Fc gamma receptors mediate antibody dependent inflammatory response and cytotoxicity as well as certain autoimmune dysfunction. We have determined the crystal structure of a human immunoglobulin receptor, FcgRIIIb, to 1.8 ? resolution. The overall fold consists of two immunoglobulin-like domains with an acute interdomain hinge angle of approximately 50 degrees. Trp 113, wedged between the N-terminal D1 and the C-terminal D2 domains, appears to further restrict the hinge angle. The putative Fc binding region of the receptor carries a net positive charge complementary to the negative charged receptor binding regions on Fc. Two separate parallel dimers are observed in the crystal lattice offering intriguing models for receptor aggregation.
| Lu, Jinghua; Marjon, Kristopher D; Mold, Carolyn et al. (2012) Pentraxins and Fc receptors. Immunol Rev 250:230-8 |
| Radaev, Sergei; Li, Sean; Sun, Peter D (2006) A survey of protein-protein complex crystallizations. Acta Crystallogr D Biol Crystallogr 62:605-12 |
| Radaev, Sergei; Sun, Peter (2002) Recognition of immunoglobulins by Fcgamma receptors. Mol Immunol 38:1073-83 |
| Radaev, S; Motyka, S; Fridman, W H et al. (2001) The structure of a human type III Fcgamma receptor in complex with Fc. J Biol Chem 276:16469-77 |
| Radaev, S; Sun, P D (2001) Recognition of IgG by Fcgamma receptor. The role of Fc glycosylation and the binding of peptide inhibitors. J Biol Chem 276:16478-83 |
| Zhang, Y; Boesen, C C; Radaev, S et al. (2000) Crystal structure of the extracellular domain of a human Fc gamma RIII. Immunity 13:387-95 |
