Abstract
Channel proteins are fundamental elements of cell function. Higher animals have a variety of channels that are activated by similar stimuli, opening with comparable kinetics, and blocked by the same drugs. Such features suggest a common evolutionary origin. Indeed, voltage-dependent calcium and potassium channels have been described in protozoa (1) and plants (2). Channels are efficacious, facilitating ion transport across the membrane with turnover numbers around 108 per second, yet selective, tightly regulated devices (3). Interpretations of the primary sequences for channel proteins suggest shared structural features. It is conceivable, therefore, that distinct properties, e.g., ionic selectivity and the sites of action of specific drugs and toxins, are contained within functional modules of similar structure that, when associated, form an operative channel protein. Such functional modules may be identifiable in the primary sequence (4–7). Accordingly, we aim to identify the principles that define the biological design of channel proteins and describe a structural motif consistent with functional characteristics of these proteins.
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Grove, A., Tomich, J.M., Montal, M. (1992). Molecular Design of Oligomeric Channel Proteins. In: Setlow, J.K. (eds) Genetic Engineering. Genetic Engineering, vol 14. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3424-2_10
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