interleukin-6 binding

Definition

Target type: molecularfunction

Binding to interleukin-6. [GOC:jl]

Interleukin-6 (IL-6) binding is a crucial step in the signaling pathway that regulates a wide range of cellular processes, including inflammation, immune responses, and cell growth. IL-6 is a pleiotropic cytokine that exerts its effects by binding to its cognate receptor, IL-6 receptor (IL-6R). The binding of IL-6 to IL-6R initiates a signaling cascade that ultimately leads to the activation of downstream transcription factors, such as STAT3, which regulate the expression of target genes.

The binding of IL-6 to IL-6R occurs in two steps:

1. **Initial Binding:** IL-6 initially binds to the soluble form of IL-6R, called soluble IL-6R (sIL-6R). This binding event is relatively weak, with a low affinity constant.

2. **Formation of the Signaling Complex:** The IL-6-sIL-6R complex then binds to a second transmembrane protein called gp130, which is a shared receptor subunit for several members of the IL-6 family cytokines. This binding event is much stronger than the initial binding of IL-6 to sIL-6R, with a high affinity constant.

The formation of the IL-6-sIL-6R-gp130 complex activates the intracellular signaling pathway, leading to the phosphorylation and activation of STAT3. Activated STAT3 translocates to the nucleus, where it binds to specific DNA sequences and regulates the transcription of target genes.

The molecular function of IL-6 binding is highly complex and involves a series of protein-protein interactions, signal transduction events, and transcriptional regulation. Understanding the molecular mechanisms underlying IL-6 binding is crucial for developing therapeutic strategies to modulate IL-6 signaling in various disease states.'
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Proteins (1)

Compounds (2)