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Interleukin‑17 receptor subunit A is a type I transmembrane glycoprotein that serves as a key component of the functional interleukin 17 (IL‑17) cytokine receptor complex. It is broadly expressed across various tissues including hematopoietic organs, bone marrow, thymus, spleen, colon, small intestine, lung tissue, and immune cells such as CD8+ T cells[1]. The extracellular region contains two fibronectin domains involved in ligand binding; intracellularly it features unique motifs including SEFIR (similar expression to fibroblast growth factor genes/IL‑1R), TILL ("TIR-like loop"), and CBAD ("C/EBPβ activation domain")[1]. Upon binding with its primary ligands—IL‑17A or IL‑17F—IL‑17RA forms a heteromeric complex with other family members like IL– 7RC to initiate proinflammatory signaling cascades critical for host defense but also implicated in chronic inflammation and autoimmunity[1][2][3].
Drugs targeting this molecule typically act by blocking the binding of interleukin 17 cytokines to their receptor, thereby inhibiting downstream proinflammatory signaling pathways that drive autoimmune and inflammatory responses.
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