Abstract
Inward rectifier K+ (IRK) channels arose early in cellular life as the combination of a pore and an immunoglobulin (Ig)-like domain. This architecture is conserved throughout the IRK family and enables regulation by different allosteric ligands (lipids, ATP, G proteins). Functional diversity in light of architectural conservation suggests that the required signal transduction functions for different ligands already existed within ancestral IRK channels. The term ‘latent allosteric capacity’ describes how new functions can emerge from conformational flexibility that arise from the combination of specific domains.
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