Abstract
Potassium channels are found in every organ and virtually in every cell, and appear to play divergent physiological roles (Hille, 1992). In the last 9 years, the identification of a number of potassium channel amino acid sequences suggests only a small number of classes with different putative membrane spanning topologies. Presently, there appear to be two major classes of K+ channels. One class, whose members include the first cloned potassium channel (Shaker) contains voltage gated channels with at least six putative hydrophobic transmembrane segments (Chandy and Gutman, 1995), including a positively charged segment and a highly conserved signature sequence (MacKinnon and Yellen, 1990, Hartmann, et al., 1991, Yool and Schwarz, 1991) in between the fifth and sixth transmembrane segment. The other class consists of smaller channels with only two putative transmembrane segments and the conserved signature sequence and whose members are mainly inward rectifiers whose rectification is a result of block of an internal particle (Ficker, et al., 1994, Lopatin, et al., 1994, Nichols, et al., 1994).
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Miller, A.G., Warren, C.A., Aldrich, R.W. (1997). Inward Rectification by an Activation Gating Mechanism. In: Latorre, R., Sáez, J.C. (eds) From Ion Channels to Cell-to-Cell Conversations. Series of the Centro de Estudios CientÃficos de Santiago. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1795-9_2
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DOI: https://doi.org/10.1007/978-1-4899-1795-9_2
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