Interleukin-17A–interleukin-17 receptor A protein–protein interaction (IL-17A:IL-17RA)

The interleukin-17A–interleukin-17 receptor A (IL-17A:IL-17RA) protein–protein interaction is a key immune signaling axis in humans, whereby the cytokine IL-17A, typically secreted by Th17 cells, binds to its high-affinity receptor IL-17RA to form a biologically active receptor complex. This interface enables downstream signaling that orchestrates the expression of pro-inflammatory mediators, making IL-17A:IL-17RA a critical contributor to host defense, tissue inflammation, and the pathogenesis of several autoimmune diseases[2][5][6][7]. The structural interaction involves IL-17A—typically a homodimer—engaging IL-17RA with high affinity, resulting in conformational changes in both molecules and often recruitment of IL-17RC for signal transduction[2][5]. Targeting this interaction with monoclonal antibodies (such as secukinumab and ixekizumab) or peptide antagonists (e.g., HAP) can successfully block signaling and ameliorate symptoms in diseases like psoriasis and ankylosing spondylitis[4][6]. Safety concerns primarily relate to blunted immune defenses against certain pathogens[5][6]. This interaction is a validated and clinically important drug target in immunology and inflammation.

Other names

IL-17A/IL-17RA complexIL17A–IL17RAinterleukin-17A–receptor A interaction

Inhibition of IL-17A binding to IL-17RA, blocking downstream signaling. Neutralization of IL-17A cytokine. Allosteric disruption of IL-17A–IL-17RA interface.