ArticleProceedings of the National Academy of Sciences of the United States of America2002
Intrinsic flexibility and gating mechanism of the potassium channel KcsA.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- PIP2-driven cytoplasmic domain motions are coupled to Kir2 channel gating.The Journal of general physiology · 2025Article
- Full opening of helix bundle crossing does not lead to NaK channel activation.The Journal of general physiology · 2022Article
- Inferring functional units in ion channel pores via relative entropy.European biophysics journal : EBJ · 2021Article
- Toward a Model for Activation of Orai Channel.iScience · 2019Article
- Targeted molecular dynamics (TMD) of the full-length KcsA potassium channel: on the role of the cytoplasmic domain in the opening process.Journal of molecular modeling · 2013Article
- Emerging approaches to probing ion channel structure and function.Neuroscience bulletin · 2012Review
- Coupling between the voltage-sensing and pore domains in a voltage-gated potassium channel.Biochimica et biophysica acta · 2012Article
- Shape-Dependent Global Deformation Modes of Large Protein Structures.Journal of molecular structure · 2010Article
- Cooperative nature of gating transitions in K(+) channels as seen from dynamic importance sampling calculations.Proteins · 2010Article
- Normal mode analysis of biomolecular structures: functional mechanisms of membrane proteins.Chemical reviews · 2010Review
- Inherent dynamics of the acid-sensing ion channel 1 correlates with the gating mechanism.PLoS biology · 2009Article
- Ion channel gates: comparative analysis of energy barriers.European biophysics journal : EBJ · 2009Article
- Conformational changes in the selectivity filter of the open-state KcsA channel: an energy minimization study.Biophysical journal · 2008Article
- Cooperative transition between open and closed conformations in potassium channels.PLoS computational biology · 2008Article
- End-point targeted molecular dynamics: large-scale conformational changes in potassium channels.Biophysical journal · 2008Article
- Inhibition mechanism of the acetylcholine receptor by alpha-neurotoxins as revealed by normal-mode dynamics.Biochemistry · 2008Article
- Nanosecond-timescale conformational dynamics of the human alpha7 nicotinic acetylcholine receptor.Biophysical journal · 2007Article
- Normal-mode refinement of anisotropic thermal parameters for potassium channel KcsA at 3.2 A crystallographic resolution.Structure (London, England : 1993) · 2007Article
- Ion conductance vs. pore gating and selectivity in KcsA channel: modeling achievements and perspectives.Journal of molecular modeling · 2007Article
- Common mechanism of pore opening shared by five different potassium channels.Biophysical journal · 2006Article
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3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The gating mechanism of the potassium channel KcsA was studied by normal mode analysis. The results provided an atomic description of the locations of the pivot points and the motional features of key structural elements in the gating process. Two pivot points were found in the motions of the inner TM2 helical bundle that directly modulate the size of the central channel pore. One point is an intrasubunit hinge point that sharply divides the structural flexibility between the more rigid selectivity filter and the more mobile peripheral transmembrane helices. Such a division is vital for KcsA because it permits the large-scale motions of transmembrane helices required for the gating and, in the meantime, maintains the rigidity of the filter region essential for the selectivity. The other pivot point is an intersubunit one at which all four TM2 helices are bundled together. During the gating process, each TM2 helix undergoes a lever-like swinging motion pivoting on the intrasubunit hinge, and the entire TM2 bundle undergoes a concerted rotational motion around the central channel axis constrained around the intersubunit bundle point. This series of motions leads to a dramatic enlargement of the intracellular gate without loosening up the structural integrity.
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