The inherent molecular property of a biological receptor that dictates which ligands (hormones, neurotransmitters) it will bind to, and the resulting downstream cellular effect, based on the precise three-dimensional fit between the ligand and the binding pocket. This specificity is fundamental to hormonal action, ensuring that signals are delivered only to appropriate target cells. Deviation from expected specificity can result in aberrant physiological signaling.
Origin
Rooted in biochemistry and pharmacology, this describes the lock-and-key principle of ligand-receptor interaction. Specificity ensures that a circulating hormone, like cortisol, activates glucocorticoid receptors (GR) but not mineralocorticoid receptors (MR) under normal conditions, despite structural similarities between the hormones.
Mechanism
The mechanism relies on the precise geometry and chemical interactions (e.g., hydrogen bonding, hydrophobic interactions) within the receptor binding domain. When a hormone binds with high affinity and appropriate conformation, it triggers signal transduction, often involving nuclear translocation and gene regulation. High specificity prevents crosstalk between different hormonal axes, maintaining the integrity of cellular response pathways.
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