Structural highlights
Function
[FCG2A_HUMAN] Binds to the Fc region of immunoglobulins gamma. Low affinity receptor. By binding to IgG it initiates cellular responses against pathogens and soluble antigens. Promotes phagocytosis of opsonized antigens.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Molecular basis for immune complex recognition: a comparison of Fc-receptor structures.,Sondermann P, Kaiser J, Jacob U J Mol Biol. 2001 Jun 8;309(3):737-49. PMID:11397093[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lu J, Marnell LL, Marjon KD, Mold C, Du Clos TW, Sun PD. Structural recognition and functional activation of FcgammaR by innate pentraxins. Nature. 2008 Dec 18;456(7224):989-92. Epub 2008 Nov 16. PMID:19011614 doi:10.1038/nature07468
- ↑ Sondermann P, Kaiser J, Jacob U. Molecular basis for immune complex recognition: a comparison of Fc-receptor structures. J Mol Biol. 2001 Jun 8;309(3):737-49. PMID:11397093 doi:10.1006/jmbi.2001.4670
