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High-affinity IgG Fc receptor I (FcγRI, also known as CD64 or hFcγRI) is the sole high-affinity receptor for IgG among Fcγ receptors, capable of binding monomeric IgG, particularly IgG1, with high affinity due to unique structural features like a hydrophobic pocket accommodating Leu235 of the Fc region and a shorter FG-loop in the D2 domain. It consists of three extracellular Ig-like domains (D1, D2, D3), forms a complex with an FcR γ-chain for signaling, and is expressed on macrophages, monocytes, neutrophils, eosinophils, and dendritic cells, with expression upregulated by interferons and IL-12. FcγRI mediates innate and adaptive immune responses through receptor clustering and signal transduction, playing key roles in immunity and links to autoimmune diseases, and its structure supports potential immunotherapy applications.
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