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[The internal symmetry of the primary structure of the beta-subunits of the tyrosine kinase receptors in insulin superfamily peptides and its relation to their functional activity].

Using the author's original graphic method, the internal symmetry of mirror type was identified in the primary structure of beta-subunit receptor tyrosine kinases of insulin superfamily peptides (receptors of insulin, insulin-like growth factor 1 and of insulin-related peptide). The most important regions of the primary structure, determining the functional activity of receptors, were shown to have the symmetrical structure. The regions are involved in receptor autophosphorylation and kinase activity form the receptor ATP-binding site, contain N-glycosylation sites, participate in the formation of intermolecular disulfide bridges with receptor alpha-subunits, and interact with other components of the signal transduction system (in particular, with G-proteins). The functionally important amino acid residues or their clusters either appear themselves the centres of internal symmetry, or are spaced in the immediate vicinity of these centres.