Abstract
Immunoreceptors play an important role in maintaining homeostasis in the body by distinguishing between self and non-self, and by acting as a starting point for immune activation and inhibition signals. However, unlike soluble proteins such as antibodies, the binding affinity between immunoreceptors and their ligands is weak and especially, the dissociation is rapid, making accurate assessment of binding affinity difficult. In this review, we focused on this weak and fast interactions in ligand recognition by immunoreceptors and introduce kinetic, thermodynamic, and structural aspects of molecular recognition mechanisms using physicochemical and structural methods.