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• W1977221331 endingPage "9022" @default.
• W1977221331 startingPage "9017" @default.
• W1977221331 abstract "Large-conductance Ca2+-voltage-activated K+ channels (BK channels) control many key physiological processes, such as neurotransmitter release and muscle contraction. A signature feature of BK channels is that they have the largest single channel conductance of all K+ channels. Here we examine the mechanism of this large conductance. Comparison of the sequence of BK channels to lower-conductance K+ channels and to a crystallized bacterial K+ channel (MthK) revealed that BK channels have a ring of eight negatively charged glutamate residues at the entrance to the intracellular vestibule. This ring of charge, which is absent in lower-conductance K+ channels, is shown to double the conductance of BK channels for outward currents by increasing the concentration of K+ in the vestibule through an electrostatic mechanism. Removing the ring of charge converts BK channels to inwardly rectifying channels. Thus, a simple electrostatic mechanism contributes to the large conductance of BK channels." @default.
• W1977221331 created "2016-06-24" @default.
• W1977221331 creator A5024563064 @default.
• W1977221331 creator A5048680925 @default.
• W1977221331 creator A5065649112 @default.
• W1977221331 date "2003-07-03" @default.
• W1977221331 modified "2023-10-15" @default.
• W1977221331 title "A ring of eight conserved negatively charged amino acids doubles the conductance of BK channels and prevents inward rectification" @default.
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• W1977221331 doi "https://doi.org/10.1073/pnas.1532257100" @default.
• W1977221331 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/166430" @default.
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