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   <subfield code="a">Activation of synaptic receptors and its allosteric regulation</subfield>
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   <subfield code="a">This review considers activation of synaptic receptors (SR) as a process of transduction of the energy of interaction between an agonist (A) and an agonist-recognizing module (R) toward an ion-conducting module (channel,Ch) orG protein within respective complexes (ARCh orARG). The agonist provides functional and, in the case of metabotropic SR, spatial association of protein components in these complexes. Conformational transformations of the latter, which are sufficient for dissociation ofG protein into subunits or opening of an ion-conducting channel, sometimes need additional energy expenditure. The source for this energy can be interaction with one more ligand: guanosine-5′-triphosphate (in the case of metabotropic SR) or glycine (in case of NMDA receptors), which act as co-agonists. The activation of SR is regulated by their allosteric modulators, which affect either the kinetics of interaction between the agonist and receptor by changing the rate of dissociation with the agonist or the kinetics of conformational transitions of the components into the activated or desensitized state.</subfield>
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