Abstract
This chapter discusses the structure and function of voltage-gated (VLG) potassium channels that are encoded by the genes related to Drosophila eag/elk/erg gene families. The eag, elk, and erg families share 47% amino acid identity in their hydrophobic cores with all sequences possessing a segment homologous to a cyclic nucleotide-binding domain. Additional localized sequence comparisons indicate that members of this family are distantly related to certain six transmembrane domain inwardly rectifying K+ channels of plant origin. Hydropathy analyses of eag, elk, and erg subfamily polypeptides suggest an S1–S6 +H5 transmembrane domain arrangement typical of those found in the voltage-gated K+ channel family. The eag/elk/erg subfamily proteins contain a positively charged amphipathic segment (S4) and a P-region. Each hydrophobic domain of eag, elk, and erg shares sequence similarity with the corresponding domain in voltage-gated K+ channels. Multiple sequence comparisons indicate a structural relationship between eag/elk/erg subfamily members to both cyclic nucleotide-gated channels and voltage-gated K+ channels.
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