ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 138 papers.
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138 citing papers in PubMed.
- Crystal structure of rice L-galactose dehydrogenase.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Potassium channels in vascular smooth muscle cells.Physiological reviews · 2026Review
- Modulation of confined water dynamics in ion channels by terahertz electric fields.Nanoscale advances · 2026Article
- HInternational journal of molecular sciences · 2025Review
- Cvill6 and Cvill7: Potent and Selective Peptide Blockers of Kv1.2 Ion Channel Isolated from Mexican ScorpionToxins · 2025Article
- Review
- Voltage sensors.Molecular pharmacology · 2025Review
- Article
- Roles of KCNA2 in Neurological Diseases: from Physiology to Pathology.Molecular neurobiology · 2024Review
- Proximity Labeling Proteomics Reveals Kv1.3 Potassium Channel Immune Interactors in Microglia.Molecular & cellular proteomics : MCP · 2024Article
- Structural Insights and Influence of Terahertz Waves in Midinfrared Region on Kv1.2 Channel Selectivity Filter.ACS omega · 2024Article
- Bioelectronic Medicine: a multidisciplinary roadmap from biophysics to precision therapies.Frontiers in integrative neuroscience · 2024Review
- Fifty years of gating currents and channel gating.The Journal of general physiology · 2023Review
- Voltage-Gated Proton Channels in the Tree of Life.Biomolecules · 2023Review
- Effect of Terahertz Electromagnetic Field on the Permeability of Potassium Channel Kv1.2.International journal of molecular sciences · 2023Article
- Novel Genetic Variants Expand the Functional, Molecular, and Pathological Diversity ofInternational journal of molecular sciences · 2023Review
- Noncanonical electromechanical coupling paths in cardiac hERG potassium channel.Nature communications · 2023Article
- Modulation of the IBBA advances · 2023Article
- Phosphatidylinositol 4,5-Bisphosphate and Cholesterol Regulators of the Calcium-Activated Chloride Channels TMEM16A and TMEM16B.Advances in experimental medicine and biology · 2023Article
- Yeast as a tool for membrane protein production and structure determination.FEMS yeast research · 2022Article
78 more citing papers are in PubMed but not listed here.
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4 authors.
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Abstract
Voltage-dependent potassium channels (Kv) are homotetramers composed of four voltage sensors and one pore domain. Because of high-level structural flexibility, the first mammalian Kv structure, Kv1.2 at 2.9 A, has about 37% molecular mass of the transmembrane portion not resolved. In this study, by applying a novel normal-mode-based X-ray crystallographic refinement method to the original diffraction data and structural model, we established the structure of full-length Kv1.2 in its native form. This structure offers mechanistic insights into voltage sensing. Particularly, it shows a hydrophobic layer of about 10 A at the midpoint of the membrane bilayer, which is likely the molecular basis for the observed "focused electric field" of Kv1.2 between the internal and external solutions. This work also demonstrated the potential of the refinement method in bringing up large chunks of missing densities, thus beneficial to structural refinement of many difficult systems.
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