| Literature DB >> 9651786 |
Abstract
The structure for the three human Fc gamma receptors classes Fc gamma RI (CD64), Fc gamma RII (CD32) and Fc gamma RIII (CD16) has been well characterized. Here the IgG binding sites on Fc gamma RII and Fc gamma RII with their responsive FG, BC and C'/E loops on the membrane proximal domains are described in detail. For Fc gamma RI the second extracellular domain is suggested as a key structure of IgG binding. The lower hinge regions of human and murine IgG binding to these Fc receptors and their structural relationship in Fc gamma R-IgG interactions are discussed. The potential of inhibiting the pathophysiological effects of Fc gamma receptors by blocking studies are considered for future therapeutic modalities.Entities:
Mesh:
Substances:
Year: 1997 PMID: 9651786 DOI: 10.3109/08830189709045703
Source DB: PubMed Journal: Int Rev Immunol ISSN: 0883-0185 Impact factor: 5.311