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Home List of Titles Biochemical analysis and crystallisation of Fc gamma RIIa, the low affinity receptor for IgG
Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/74771
- Biochemical analysis and crystallisation of Fc gamma RIIa, the low affinity receptor for IgG
- Powell, M. S.; Barton, P. A.; Emmanouilidis, D.; Wines, B. D.; Neumann, G. M.; Peitersz, G. A.; Maxwell, K. F.; Garrett, T. P.; Hogarth, P. M.
- FcgRIIa is one of a family of specific cell surface receptors for immunoglobulin. FcgRIIa, which binds immune complexes of certain IgG isotypes, plays important roles in immune homeostasis. However, the precise characteristics of IgG binding and three-dimensional structure of FcgRIIa have not been reported. This study describes the affinity of the FcgRIIa:IgG interaction as well as biochemical characterisation of recombinant FcgRIIa that has been used to generate high quality crystals. Equilibrium mammalian and insect cell derived FcgRIIa established the genuine N-terminus with Q being the first amino acid in the sequence Q, A, A, A, P ... extending the N-terminus further than previously thought. Furthermore, both potential N-linked glycosylation sites are occupied. Electrospray ionisation mass spectrometry (ESMS) indicate that the N-glycans of baculovirus derived FcgRIIa are core mannose oligosaccharide side chains. Finally, we describe the first crystallisation of diffraction quality crystals of soluble FcgRIIa. Orthorhombic crystals diffract X-rays beyond 2.1 A° resolution in the space group P21212 with cell dimensions a=78.8 A°, b=100.5 A°, c=27.8 A°. This marks a significant advance towards understanding the three-dimensional structure of FcgRIIa and related FcR proteins that share high amino acid identity with FcgRIIa.
- Publication type
- Journal article
- Research centre
- Swinburne University of Technology. School of Engineering and Science
- Immunology Letters, Vol. 68, no. 1 (May 1999), pp. 17-23
- Publication year
- Crystallisation; Fc receptors; Inflammation
- Elsevier B.V.
- Publisher URL
- Copyright © 1999 Elsevier Science B.V. All rights reserved.
- Peer reviewed