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Dynamic measurements for funny channels

Proteins possess the uncanny ability to telegraph signals over long distances. The presence of a ligand, snugly bound to a site on one end of a molecule, can be “felt” by an effector domain several nanometers away. Determining precisely how this task is accomplished is a major challenge for structural biologists. Hypotheses range from the purely dynamic—for example, a binding event affects the conformational possibilities of nearby domains—to the mechanical view whereby a series of structural changes propagates like dominoes from one domain to the next. In PNAS, Saponaro et al. use NMR spectroscopy to examine the first steps in the process that transduces ligand binding into opening of a hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channel and present a structural basis for the inhibition of HCN by the accessory protein TRIP8b (tetratricopeptide repeat-containing Rab8b-interacting protein) (1).