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Unlock the insights into mIL17 A/F, a pivotal glycoprotein in human physiology, meticulously crafted as a disulfide-linked heterodimer. This potent molecule combines the dynamic forces of IL-17A and IL-17F, members of the IL-17 family, to orchestrate vital biological functions. Embodied within the cysteine knot motif are the intricate structures of these proteins, adorned with essential disulfide bonds. Human IL-17A and IL-17F emerge as precursors, each bearing unique signal sequences and glycosylation sites, culminating in their distinct roles in cellular signaling. Sharing 50% amino acid sequence identity, these proteins exhibit a remarkable affinity with mouse IL-17A and IL-17F, illuminating the evolutionary thread woven through interleukin biology. Activated CD4+ T cells, known as Th17, are the craftsmen behind the production of IL-17A/F homodimers, under the directive influence of IL-23. This finely tuned mechanism relies on the collaboration between IL17RA and IL17RC, forming a heterodimer essential for the binding of IL-17A and IL-17F. The resultant IL-17A/F complex triggers chemokine production and fosters airway neutrophilia, showcasing its pivotal role with intermediate potency between IL-17A and IL-17F. Explore the intricate dynamics of mIL17 A/F for unparalleled insights into immune regulation and therapeutic potential.