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This review discusses the gating, permeability, and modulation properties of the viral potassium channel Kcv, comparing them to bacterial and mammalian K+ channels.
This review summarizes the structural and functional features of the viral potassium channel Kcv, comparing it to bacterial and mammalian channels.
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Provides minimal K+ channel model; leaves open relevance to cardiac electrophysiology.
The chlorella virus PBCV-1 was the first virus found to encode a functional potassium channel protein (Kcv). Kcv is small (94 aa) and basically consists of the M1-P-M2 (membrane-pore-membrane) module typical of the pore regions of all known potassium channels. Kcv forms functional channels in three heterologous systems. This brief review discusses the gating, permeability and modulation properties of Kcv and compares them to the properties of bacterial and mammalian K+ channels.
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Gazzarrini et al. (2003) reported a review. Kcv (viral potassium channel) vs. Bacterial and mammalian K+ channels was evaluated. This review discusses the gating, permeability, and modulation properties of the viral potassium channel Kcv, comparing them to bacterial and mammalian K+ channels.
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