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- PDB-7ukh: Human Kv4.2-KChIP2-DPP6 channel complex in an open state, intrace... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7ukh | ||||||
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Title | Human Kv4.2-KChIP2-DPP6 channel complex in an open state, intracellular region | ||||||
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![]() | MEMBRANE PROTEIN / potassium channel complex | ||||||
Function / homology | ![]() ER retention sequence binding / positive regulation of voltage-gated potassium channel activity / Kv4.2-KChIP2 channel complex / clustering of voltage-gated potassium channels / A-type (transient outward) potassium channel activity / Phase 1 - inactivation of fast Na+ channels / positive regulation of potassium ion export across plasma membrane / voltage-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / potassium channel complex / membrane repolarization during cardiac muscle cell action potential ...ER retention sequence binding / positive regulation of voltage-gated potassium channel activity / Kv4.2-KChIP2 channel complex / clustering of voltage-gated potassium channels / A-type (transient outward) potassium channel activity / Phase 1 - inactivation of fast Na+ channels / positive regulation of potassium ion export across plasma membrane / voltage-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / potassium channel complex / membrane repolarization during cardiac muscle cell action potential / potassium ion export across plasma membrane / membrane repolarization / Voltage gated Potassium channels / regulation of potassium ion transmembrane transport / postsynaptic specialization membrane / anchoring junction / action potential / regulation of heart contraction / neuronal cell body membrane / voltage-gated potassium channel activity / potassium channel activity / plasma membrane raft / locomotor rhythm / detection of calcium ion / GABA-ergic synapse / potassium channel regulator activity / neuronal action potential / potassium ion transmembrane transport / voltage-gated potassium channel complex / sensory perception of pain / muscle contraction / potassium ion transport / protein homooligomerization / cellular response to hypoxia / chemical synaptic transmission / postsynaptic membrane / perikaryon / transmembrane transporter binding / dendritic spine / neuronal cell body / glutamatergic synapse / synapse / calcium ion binding / dendrite / protein-containing complex binding / signal transduction / identical protein binding / metal ion binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.33 Å | ||||||
![]() | Zhao, H. / Dai, Y. / Lee, C.H. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Activation and closed-state inactivation mechanisms of the human voltage-gated K4 channel complexes. Authors: Wenlei Ye / Hongtu Zhao / Yaxin Dai / Yingdi Wang / Yu-Hua Lo / Lily Yeh Jan / Chia-Hsueh Lee / ![]() Abstract: The voltage-gated ion channel activity depends on both activation (transition from the resting state to the open state) and inactivation. Inactivation is a self-restraint mechanism to limit ion ...The voltage-gated ion channel activity depends on both activation (transition from the resting state to the open state) and inactivation. Inactivation is a self-restraint mechanism to limit ion conduction and is as crucial to membrane excitability as activation. Inactivation can occur when the channel is open or closed. Although open-state inactivation is well understood, the molecular basis of closed-state inactivation has remained elusive. We report cryo-EM structures of human K4.2 channel complexes in inactivated, open, and closed states. Closed-state inactivation of K4 involves an unprecedented symmetry breakdown for pore closure by only two of the four S4-S5 linkers, distinct from known mechanisms of open-state inactivation. We further capture K4 in a putative resting state, revealing how voltage sensor movements control the pore. Moreover, our structures provide insights regarding channel modulation by KChIP2 and DPP6 auxiliary subunits. Our findings elucidate mechanisms of closed-state inactivation and voltage-dependent activation of the K4 channel. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 299.3 KB | Display | ![]() |
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PDB format | ![]() | 232.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 56.1 KB | Display | |
Data in CIF | ![]() | 75.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 26581MC ![]() 7uk5C ![]() 7ukcC ![]() 7ukdC ![]() 7ukeC ![]() 7ukfC ![]() 7ukgC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 59049.332 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein | Mass: 28975.486 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #3: Chemical | ChemComp-ZN / #4: Chemical | ChemComp-CA / Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Human Kv4.2-KChIP2-DPP6 channel complex in an open state, intracellular region Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1600 nm / Nominal defocus min: 600 nm |
Image recording | Electron dose: 85.9 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
CTF correction | Type: NONE |
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3D reconstruction | Resolution: 2.33 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 278343 / Symmetry type: POINT |