ArticleProceedings of the National Academy of Sciences of the United States of America2005
Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 papers.
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Who cites it
166 citing papers in PubMed.
- B-cell epitope prediction in the age of machine learning: advancements and challenges.Journal of translational medicine · 2026Review
- Enhanced Site-Specific Fluorescent Labeling of Membrane Proteins Using Native Nanodiscs.Biomolecules · 2025Article
- Cholesterol modulates the structural dynamics of the paddle motif loop of KvAP voltage sensor.Current research in structural biology · 2024Article
- The unique structural characteristics of the Kir 7.1 inward rectifier potassium channel: a novel player in energy homeostasis control.American journal of physiology. Cell physiology · 2023Review
- Cell-Free Synthesis and Electrophysiological Analysis of Multipass Voltage-Gated Ion Channels Tethered in Microsomal Membranes.Advances in biochemical engineering/biotechnology · 2023Article
- A mutation in the S6 segment of the KvAP channel changes the secondary structure and alters ion channel activity in a lipid bilayer membrane.Amino acids · 2022Article
- The 70-year search for the voltage-sensing mechanism of ion channels.The Journal of physiology · 2022Article
- CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021Review
- Structure of membrane diacylglycerol kinase in lipid bilayers.Communications biology · 2021Article
- External Cd2+ and protons activate the hyperpolarization-gated K+ channel KAT1 at the voltage sensor.The Journal of general physiology · 2021Article
- High-Resolution Structures of KHandbook of experimental pharmacology · 2021Article
- Inferring functional units in ion channel pores via relative entropy.European biophysics journal : EBJ · 2021Article
- The membrane protein KCNQ1 potassium ion channel: Functional diversity and current structural insights.Biochimica et biophysica acta. Biomembranes · 2020Review
- Illuminating Voltage Sensor Paddling in Different Membrane Milieu.Biophysical journal · 2020Article
- Structural Dynamics of the Paddle Motif Loop in the Activated Conformation of KvAP Voltage Sensor.Biophysical journal · 2020Article
- Non-linear Conductance, Rectification, and Mechanosensitive Channel Formation of Lipid Membranes.Frontiers in cell and developmental biology · 2020Article
- Cryo-EM structure of the KvAP channel reveals a non-domain-swapped voltage sensor topology.eLife · 2019Article
- Voltage-Dependent Profile Structures of a Kv-Channel via Time-Resolved Neutron Interferometry.Biophysical journal · 2019Article
- The neuropeptide GsMTx4 inhibits a mechanosensitive BK channel through the voltage-dependent modification specific to mechano-gating.The Journal of biological chemistry · 2019Article
- NMR Structural Analysis of Isolated Shaker Voltage-Sensing Domain in LPPG Micelles.Biophysical journal · 2019Article
106 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
Abstract
Voltage-dependent ion channels gate open in response to changes in cell membrane voltage. This form of gating permits the propagation of action potentials. We present two structures of the voltage-dependent K(+) channel KvAP, in complex with monoclonal Fv fragments (3.9 A) and without antibody fragments (8 A). We also studied KvAP with disulfide cross-bridges in lipid membranes. Analyzing these data in the context of the crystal structure of Kv1.2 and EPR data on KvAP we reach the following conclusions: (i) KvAP is similar in structure to Kv1.2 with a very modest difference in the orientation of its voltage sensor; (ii) mAb fragments are not the source of non-native conformations of KvAP in crystal structures; (iii) because KvAP contains separate loosely adherent domains, a lipid membrane is required to maintain their correct relative orientations, and (iv) the model of KvAP is consistent with the proposal of voltage sensing through the movement of an arginine-containing helix-turn-helix element at the protein-lipid interface.
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