ArticleThe Journal of membrane biology2006
Elongation of outer transmembrane domain alters function of miniature K+ channel Kcv.
Article in The Journal of membrane biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Modular architecture of KEMBO reports · 2025Review
- How to resolve microsecond current fluctuations in single ion channels: the power of beta distributions.Channels (Austin, Tex.) · 2015Review
- Salt bridges in the miniature viral channel Kcv are important for function.European biophysics journal : EBJ · 2010Article
- Model development for the viral Kcv potassium channel.Biophysical journal · 2009Article
- Transmembrane domain length of viral K+ channels is a signal for mitochondria targeting.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Electrokinetics of miniature K+ channel: open-state V sensitivity and inhibition by K+ driving force.The Journal of membrane biology · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
The virus-coded channel Kcv has the typical structure of a two-transmembrane domain K(+) channel. Exceptional are its cytoplasmic domains: the C terminus basically ends inside the membrane and, hence, precludes the formation of a cytoplasmic gate by the so-called bundle crossing; the cytoplasmic N terminus is composed of only 12 amino acids. According to structural predictions, it is positioned in the membrane/aqueous interface and connected via a proline kink to the outer transmembrane domain (TM1). Here, we show that this proline kink affects channel function by determining the position of TM1 in the membrane bilayer. Extension of the hydrophobic length of TM1 by either eliminating the proline kink or introducing an alanine in TM1 augments a time- and voltage-dependent inward rectification of the channel. This suggests that the positional information of TM1 in the bilayer is transmitted to a channel gate, which is not identical with the cytoplasmic bundle crossing.
Indexed as
Identifiers
16708260What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.