high-affinity IgG receptor activity
Definition
Target type: molecularfunction
Combining with high affinity with an immunoglobulin of an IgG isotype via the Fc region, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. [GOC:add, GOC:signaling, ISBN:0781735149]
High-affinity IgG receptor activity, also known as FcγRI or CD64, is a molecular function that describes the ability of a protein to bind to the Fc region of immunoglobulin G (IgG) antibodies with high affinity. This binding event is crucial for the initiation of antibody-dependent cellular cytotoxicity (ADCC), a process where immune cells like natural killer (NK) cells and macrophages recognize and eliminate target cells coated with IgG antibodies. The high-affinity binding of IgG to FcγRI triggers a cascade of intracellular signaling events leading to the activation of effector functions such as phagocytosis, antibody-dependent cellular cytotoxicity, and cytokine production. FcγRI is predominantly expressed on immune cells like macrophages, neutrophils, and monocytes, enabling them to effectively engage in antibody-mediated immune responses.'
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Proteins (1)
| Protein | Definition | Taxonomy |
|---|---|---|
| High affinity immunoglobulin gamma Fc receptor I | A high affinity immunoglobulin gamma Fc receptor I that is encoded in the genome of human. [PRO:CNA, UniProtKB:P12314] | Homo sapiens (human) |
Compounds (2)
| Compound | Definition | Classes | Roles |
|---|---|---|---|
| bms 777607 | N-(4-(2-amino-3-chloropyridin-4-yloxy)-3-fluorophenyl)-4-ethoxy-1-(4-fluorophenyl)-2-oxo-1,2-dihydropyridine-3-carboxamide: a Met kinase inhibitor; structure in first source | aromatic amide | |
| nms p937 | NMS P937: a polo-like kinase 1 inhibitor; structure in first source |