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.

National Institute of Health (NIH)
National Institute of Allergy and Infectious Diseases (NIAID)
Intramural Research (Z01)
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