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- EMDB-26581: Human Kv4.2-KChIP2-DPP6 channel complex in an open state, intrace... -
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Open data
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Basic information
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Title | Human Kv4.2-KChIP2-DPP6 channel complex in an open state, intracellular region | |||||||||
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![]() | potassium channel complex / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() ER retention sequence binding / positive regulation of voltage-gated potassium channel activity / Kv4.2-KChIP2 channel complex / A-type (transient outward) potassium channel activity / Phase 1 - inactivation of fast Na+ channels / clustering of voltage-gated potassium 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 / A-type (transient outward) potassium channel activity / Phase 1 - inactivation of fast Na+ channels / clustering of voltage-gated potassium 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 / anchoring junction / postsynaptic specialization membrane / regulation of heart contraction / neuronal cell body membrane / voltage-gated potassium channel activity / plasma membrane raft / action potential / locomotor rhythm / potassium channel activity / neuronal action potential / detection of calcium ion / potassium channel regulator activity / GABA-ergic synapse / muscle contraction / voltage-gated potassium channel complex / potassium ion transmembrane transport / sensory perception of pain / 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 / dendrite / calcium ion binding / protein-containing complex binding / signal transduction / identical protein binding / metal ion binding / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.33 Å | |||||||||
![]() | Zhao H / Dai Y / Lee CH | |||||||||
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
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 398.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 15.1 KB 15.1 KB | Display Display | ![]() |
Images | ![]() | 107.1 KB | ||
Filedesc metadata | ![]() | 5.6 KB | ||
Others | ![]() ![]() | 390.9 MB 390.9 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7ukhMC ![]() 7uk5C ![]() 7ukcC ![]() 7ukdC ![]() 7ukeC ![]() 7ukfC ![]() 7ukgC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 0.826 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
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Projections & Slices |
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Density Histograms |
-Half map: #2
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Density Histograms |
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Sample components
-Entire : Human Kv4.2-KChIP2-DPP6 channel complex in an open state, intrace...
Entire | Name: Human Kv4.2-KChIP2-DPP6 channel complex in an open state, intracellular region |
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Components |
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-Supramolecule #1: Human Kv4.2-KChIP2-DPP6 channel complex in an open state, intrace...
Supramolecule | Name: Human Kv4.2-KChIP2-DPP6 channel complex in an open state, intracellular region type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Potassium voltage-gated channel subfamily D member 2
Macromolecule | Name: Potassium voltage-gated channel subfamily D member 2 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 59.049332 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MAAGVAAWLP FARAAAIGWM PVASGPMPAP PRQERKRTQD ALIVLNVSGT RFQTWQDTLE RYPDTLLGSS ERDFFYHPET QQYFFDRDP DIFRHILNFY RTGKLHYPRH ECISAYDEEL AFFGLIPEII GDCCYEEYKD RRRENAERLQ DDADTDTAGE S ALPTMTAR ...String: MAAGVAAWLP FARAAAIGWM PVASGPMPAP PRQERKRTQD ALIVLNVSGT RFQTWQDTLE RYPDTLLGSS ERDFFYHPET QQYFFDRDP DIFRHILNFY RTGKLHYPRH ECISAYDEEL AFFGLIPEII GDCCYEEYKD RRRENAERLQ DDADTDTAGE S ALPTMTAR QRVWRAFENP HTSTMALVFY YVTGFFIAVS VIANVVETVP CGSSPGHIKE LPCGERYAVA FFCLDTACVM IF TVEYLLR LAAAPSRYRF VRSVMSIIDV VAILPYYIGL VMTDNEDVSG AFVTLRVFRV FRIFKFSRHS QGLRILGYTL KSC ASELGF LLFSLTMAII IFATVMFYAE KGSSASKFTS IPAAFWYTIV TMTTLGYGDM VPKTIAGKIF GSICSLSGVL VIAL PVPVI VSNFSRIYHQ NQRADKRRAQ KKARLARIRA AKSGSANAYM QSKRNGLLSN QLQSSEDEQA FVSKSGSSFE TQHHH LLHC LEKTTNHEFV DEQVFEESCM EVATVNRPSS HSPSLSSQQG UniProtKB: A-type voltage-gated potassium channel KCND2 |
-Macromolecule #2: Isoform 2 of Kv channel-interacting protein 2
Macromolecule | Name: Isoform 2 of Kv channel-interacting protein 2 / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 28.975486 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MRGQGRKESL SDSRDLDGSY DQLTGHPPGP TKKALKQRFL KLLPCCGPQA LPSVSENSVD DEFELSTVCH RPEGLEQLQE QTKFTRKEL QVLYRGFKNE CPSGIVNEEN FKQIYSQFFP QGDSSTYATF LFNAFDTNHD GSVSFEDFVA GLSVILRGTV D DRLNWAFN ...String: MRGQGRKESL SDSRDLDGSY DQLTGHPPGP TKKALKQRFL KLLPCCGPQA LPSVSENSVD DEFELSTVCH RPEGLEQLQE QTKFTRKEL QVLYRGFKNE CPSGIVNEEN FKQIYSQFFP QGDSSTYATF LFNAFDTNHD GSVSFEDFVA GLSVILRGTV D DRLNWAFN LYDLNKDGCI TKEEMLDIMK SIYDMMGKYT YPALREEAPR EHVESFFQKM DRNKDGVVTI EEFIESCQKD EN IMRSMQL FDNVI UniProtKB: A-type potassium channel modulatory protein KCNIP2 |
-Macromolecule #3: ZINC ION
Macromolecule | Name: ZINC ION / type: ligand / ID: 3 / Number of copies: 4 / Formula: ZN |
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Molecular weight | Theoretical: 65.409 Da |
-Macromolecule #4: CALCIUM ION
Macromolecule | Name: CALCIUM ION / type: ligand / ID: 4 / Number of copies: 12 / Formula: CA |
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Molecular weight | Theoretical: 40.078 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 85.9 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.6 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 2.33 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 278343 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |