Please use this identifier to cite or link to this item:
|Title:||Alteration of the Fc gamma RIIa dimer interface affects receptor signaling but not ligand binding.|
|Authors:||Powell, Maree S;Barnes, Nadine C;Bradford, Tessa M;Musgrave, Ian F;Wines, Bruce D;Cambier, John C;Hogarth, P Mark|
|Affiliation:||The Macfarlane Burnet Institute for Medical Research and Public Health Limited, Austin Health, Heidelberg, Victoria, Australia.|
|Citation:||Journal of Immunology (baltimore, Md. : 1950); 176(12): 7489-94|
|Abstract:||The aggregation of cell surface FcRs by immune complexes induces a number of important Ab-dependent effector functions. However, despite numerous studies that examine receptor function, very little is known about the molecular organization of these receptors within the cell. In this study, protein complementation, mutagenesis, and ligand binding analyses demonstrate that human FcgammaRIIa is present as a noncovalent dimer form. Protein complementation studies found that FcgammaRIIa molecules are closely associated. Mutagenesis of the dimer interface, as identified by crystallographic analyses, did not affect ligand binding yet caused significant alteration to the magnitude and kinetics of receptor phosphorylation. The data suggest that the ligand binding and the dimer interface are distinct regions within the receptor, and noncovalent dimerization of FcgammaRIIa may be an essential feature of the FcgammaRIIa signaling cascade.|
|Internal ID Number:||16751395|
|Appears in Collections:||Journal articles|
Files in This Item:
There are no files associated with this item.
Items in AHRO are protected by copyright, with all rights reserved, unless otherwise indicated.