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Interleukin-17 receptor A (IL-17RA) is a ubiquitous type I transmembrane glycoprotein and the founding member of the IL-17 receptor family [6, 15]. It serves as a common signaling subunit that forms heterodimeric complexes with other family members, such as IL-17RC, IL-17RE, or IL-17RB, to mediate the effects of various IL-17 cytokines including IL-17A, IL-17F, IL-17C, and IL-17E [1, 18]. Biologically, IL-17RA is essential for host defense against extracellular bacteria and fungi by inducing the production of proinflammatory cytokines, chemokines, and antimicrobial peptides [10, 12]. However, dysregulated IL-17RA signaling is a key driver of chronic inflammatory and autoimmune diseases, most notably plaque psoriasis, psoriatic arthritis, and ankylosing spondylitis [7, 8]. In the pharmaceutical landscape, IL-17RA is a validated therapeutic target; the monoclonal antibody brodalumab directly binds to and inhibits the receptor, effectively blocking multiple IL-17 isoforms [1, 14]. While highly effective for skin and joint inflammation, therapeutic modulation of IL-17RA carries risks such as increased susceptibility to mucocutaneous candidiasis and potential exacerbation of inflammatory bowel disease [2, 13].
Antagonist; Monoclonal antibody that binds to the extracellular domain of IL-17RA, blocking the binding of IL-17A, IL-17F, IL-17A/F heterodimers, IL-17C, and IL-17E (IL-25) [1, 18].
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