| Autor: |
Hogarth, P. Mark, Ierino, Frank L., Hulett, Mark D. |
| Zdroj: |
ImmunoMethods; February 1994, Vol. 4 Issue: 1 p17-24, 8p |
| Abstrakt: |
The low-affinity receptor for IgG, FcγRll, and the high-affinity receptor for IgE, FcεRI, are functionally distinct but structurally homologous receptors. These characteristics have been exploited using a chimeric receptor strategy to examine segments of human FcγRII for IgG-binding function. A series of chimeric receptors was generated by exchanging coding regions of the extracellular ligand-binding regions between FcγRll and the FcεRI α chain using splice overlap extension by the polymerase chain reaction. The expression of these chimeric receptors in COS-7 cells and analysis of their IgG/IgE binding capacities have enabled the Ig-binding region of FcγRll to be localized to a subregion of the second extracellular domain. The localization of the Ig-binding region of FcγRII has provided the opportunity of performing site-directed mutagenesis to determine the key amino acids involved in the interaction of the receptor with IgG. These findings demonstrate that the chimeric receptor approach is a powerful technique for the dissection of structure/function relationships of structurally related yet functionally different molecules.Copyright 1994, 1999 Academic Press |
| Databáze: |
Supplemental Index |
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