kappa-type opioid receptor binding

Definition

Target type: molecularfunction

Binding to a kappa-type opioid receptor. [GOC:mah, GOC:nln]

Kappa-type opioid receptors (KORs) are G protein-coupled receptors that mediate the physiological effects of the endogenous opioid peptides dynorphin and endomorphin, as well as exogenous opioid drugs such as the synthetic opioid ketocyclazocine. Upon ligand binding, KORs activate a signaling cascade involving the heterotrimeric G protein Gi/o, which in turn inhibits adenylate cyclase activity, leading to a decrease in intracellular cAMP levels. This pathway can lead to a variety of cellular responses, including modulation of neuronal excitability, pain perception, and reward pathways. KORs are also implicated in the regulation of stress responses, anxiety, and addiction. The molecular function of KOR binding involves a complex interplay of receptor structure, ligand binding, and downstream signaling events. The receptor's seven transmembrane domains are responsible for the binding of opioid ligands. Upon ligand binding, the receptor undergoes a conformational change that activates its intracellular signaling domains. This activation triggers the interaction with Gi/o proteins, leading to the inhibition of adenylate cyclase and the activation of other intracellular signaling pathways. The specific molecular events involved in KOR activation and signaling are still under investigation, but it is clear that the binding of ligands to the receptor is a crucial step in the process.'
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Proteins (1)

Compounds (7)