Receptor Ligand Interaction is the fundamental biochemical process describing the highly specific, non-covalent binding of a signaling molecule (the ligand, such as a hormone or neurotransmitter) to a complementary protein structure (the receptor) located on or within a target cell. This molecular recognition event is the initial, critical step in all hormonal and cellular communication, triggering a cascade of intracellular events that ultimately leads to a specific physiological response. The strength and duration of this interaction dictate the magnitude of the biological signal.
Origin
This core concept originates from molecular biology and pharmacology, formalized by the “lock-and-key” model proposed by Emil Fischer and later refined by the “induced fit” model. The term is etymologically derived from “receptor,” meaning to receive, and “ligand,” meaning to bind. It is the central paradigm for understanding how therapeutic agents, including exogenous hormones and peptides, exert their effects on the human body.
Mechanism
The interaction begins when the ligand’s three-dimensional structure fits precisely into the receptor’s binding pocket, initiating a conformational change in the receptor protein. This structural change acts as a switch, activating an intracellular signaling pathway, which may involve G-proteins, enzyme cascades, or the direct translocation of the receptor-ligand complex to the cell nucleus. The cellular response is terminated when the ligand dissociates or the complex is internalized and degraded.
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