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  • 标题:A ring of eight conserved negatively charged amino acids doubles the conductance of BK channels and prevents inward rectification
  • 本地全文:下载
  • 作者:Tinatin I. Brelidze ; Xiaowei Niu ; Karl L. Magleby
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2003
  • 卷号:100
  • 期号:15
  • 页码:9017-9022
  • DOI:10.1073/pnas.1532257100
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要: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.
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