ArticleEuropean biophysics journal : EBJ2004
Arranging the elements of the potassium channel: the T1 domain occludes the cytoplasmic face of the channel.
Article in European biophysics journal : EBJ, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Genomic insights into the virulence and salt tolerance of Staphylococcus equorum.Scientific reports · 2017Article
- Cytoplasmic domains and voltage-dependent potassium channel gating.Frontiers in pharmacology · 2012Article
- Potassium channel opening: a subtle two-step.The Journal of physiology · 2009Article
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Authors and funding
3 authors.
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Abstract
The voltage-gated potassium channel is currently one of the few membrane proteins where functional roles have been mapped onto specific segments of sequence. Although high-resolution structures of the transmembrane portions of three bacterial potassium channels, the tetramerization domain and the cytoplasmic "ball" are available, their relative spatial arrangement in mammalian channels remains a matter of ongoing debate. Cryo-electron microscopic images of the six transmembrane voltage-gated Kv channel have been reconstructed at up to 18 A resolution, revealing that the T1 domain tetramerizes and is suspended below the transmembrane segments. However, the resolution of these images is insufficient to reveal the location of the third piece of the puzzle, the inactivating ball domain. We have used the aberrant interactions observed in a series of chimaeric channels to establish that an assembled T1 domain restricts access to the cytoplasmic face of the channel, suggesting that the N-terminal "ball and chain" may be confined in the space between the T1 domain and the transmembrane portion of the channel.
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