ArticleEuropean biophysics journal : EBJ2010
Salt bridges in the miniature viral channel Kcv are important for function.
Article in European biophysics journal : EBJ, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Modular architecture of KEMBO reports · 2025Review
- How physical forces drive the process of helical membrane protein folding.EMBO reports · 2022Review
- Chloroviruses.Viruses · 2019Review
- All-atom virus simulations.Current opinion in virology · 2018Review
- Exploring the Viral Channel KcvThe Journal of membrane biology · 2018Article
- How to resolve microsecond current fluctuations in single ion channels: the power of beta distributions.Channels (Austin, Tex.) · 2015Review
- Potassium ion channels: could they have evolved from viruses?Plant physiology · 2013Review
- Chloroviruses: not your everyday plant virus.Trends in plant science · 2012Review
- Isoflurane alters the structure and dynamics of GLIC.Biophysical journal · 2011Article
- Viral proteins function as ion channels.Biochimica et biophysica acta · 2011Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The viral potassium channel Kcv comprises only 94 amino acids, which represent the pore module of more complex K(+) channels. As for Kir-type channels, Kcv also has a short N-terminal helix exposed to the cytoplasm, upstream of the first transmembrane domain. Here we show that this helix is relevant for Kcv function. The presence of charged amino acids, which form dynamic inter- and intra-subunit salt bridges is crucial. Electrophysiological measurements, yeast rescue experiments and molecular dynamics simulations show that mutants in which the critical salt bridge formation is impaired have no or reduced channel activity. We conclude that these salt bridges destabilise the complexation of K(+) ions by negative charges on the inner transmembrane domain at the entrance into the cavity. This feature facilitates a continuous and coordinated transfer of ions between the cavity and the cytoplasm for channels without the canonical bundle crossing.
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Registered trials
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