Molecular basis for immune complex recognition: a comparison of Fc-receptor structures.
Once antigen is opsonised by IgG it is removed from the circulation by Fcgamma-receptor expressing cells. Fcgamma-receptors are type I transmembrane molecules that carry extracellular parts consisting of two or three immunoglobulin domains. Previously solved structures of Fc-receptors reveal that the N-terminal two Ig-like domains are arranged in a steep angle forming a heart-shaped structure. The crystal structure of the FcgammaRIII/hIgG1-Fc-fragment demonstrated that the Fc-fragment is recognised through loops of the C-terminal receptor domain of the FcgammaRIII. As the overall structure of the FcRs and their Ig ligands are very similar we modelled the Ig complexes with FcgammaRI, FcgammaRII and FcepsilonRIalpha based on the FcgammaRIII/hIgG1-Fc-fragment structure. The obtained models are consistent with the observed biochemical data and may explain the observed specificity and affinities.
Sondermann
P
P
Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, Martinsried, D-82152, Germany. sonderma@biochem.mpg.de
Kaiser
J
J
Jacob
U
U
D000595:Amino Acid Sequence; D000936:Antigen-Antibody Complex / Q000737:chemistry* / Q000276:immunology*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006801:Humans; D007073:Immunoglobulin E / Q000737:chemistry / Q000276:immunology; D007141:Immunoglobulin Fc Fragments / Q000737:chemistry / Q000276:immunology; D007074:Immunoglobulin G / Q000737:chemistry / Q000276:immunology; D007136:Immunoglobulins / Q000737:chemistry* / Q000276:immunology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017452:Receptors, IgG / Q000737:chemistry* / Q000276:immunology*; D016415:Sequence Alignment; D012995:Solubility; D013379:Substrate Specificity; D013816:Thermodynamics
D000936:Antigen-Antibody Complex; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D007136:Immunoglobulins; D017452:Receptors, IgG; D007073:Immunoglobulin E