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- PDB-24vj: Cryo-EM structure of the human KCNQ2/KCNQ3 heterotetramer (3:1 st... -

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Basic information

Entry
Database: PDB / ID: 24vj
TitleCryo-EM structure of the human KCNQ2/KCNQ3 heterotetramer (3:1 stoichiometry) with CLM142 (M2223 CLM142, without symmetry expansion)
Components
  • Green fluorescent protein,Potassium voltage-gated channel subfamily KQT member 2
  • Potassium voltage-gated channel subfamily KQT member 3
KeywordsMEMBRANE PROTEIN / potassium channels
Function / homology
Function and homology information


axon initial segment / Voltage gated Potassium channels / node of Ranvier / ankyrin binding / Interaction between L1 and Ankyrins / voltage-gated monoatomic cation channel activity / action potential / voltage-gated potassium channel activity / voltage-gated potassium channel complex / potassium ion transmembrane transport ...axon initial segment / Voltage gated Potassium channels / node of Ranvier / ankyrin binding / Interaction between L1 and Ankyrins / voltage-gated monoatomic cation channel activity / action potential / voltage-gated potassium channel activity / voltage-gated potassium channel complex / potassium ion transmembrane transport / bioluminescence / generation of precursor metabolites and energy / nervous system development / chemical synaptic transmission / calmodulin binding / synapse / cell surface / membrane / plasma membrane
Similarity search - Function
Potassium channel, voltage dependent, KCNQ3 / Potassium channel, voltage dependent, KCNQ2 / Unstructured region on Potassium channel subunit alpha KvLQT2 / Ankyrin-G binding site / Ankyrin-G binding motif of KCNQ2-3 / Potassium channel, voltage dependent, KCNQ / Potassium channel, voltage dependent, KCNQ, C-terminal / KCNQ voltage-gated potassium channel / Green fluorescent protein, GFP / Green fluorescent protein-related ...Potassium channel, voltage dependent, KCNQ3 / Potassium channel, voltage dependent, KCNQ2 / Unstructured region on Potassium channel subunit alpha KvLQT2 / Ankyrin-G binding site / Ankyrin-G binding motif of KCNQ2-3 / Potassium channel, voltage dependent, KCNQ / Potassium channel, voltage dependent, KCNQ, C-terminal / KCNQ voltage-gated potassium channel / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Ion transport domain / Ion transport protein
Similarity search - Domain/homology
Chem-9PE / : / Chem-YJ0 / Potassium voltage-gated channel subfamily KQT member 3 / Potassium voltage-gated channel subfamily KQT member 2 / Green fluorescent protein
Similarity search - Component
Biological speciesHomo sapiens (human)
Aequorea victoria (jellyfish)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.07 Å
AuthorsWang, Y.F. / Yang, H. / Qu, Y.N. / Shen, H.Z.
Funding support China, 1items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China) China
CitationJournal: Vita / Year: 2026
Title: Structural basis for heteromeric assembly and subthreshold activation of human M-channel
Authors: Wang, Y. / Yang, H. / Qu, Y. / Li, J. / Li, X. / Hou, W. / Wu, K. / Xie, G. / Wang, X. / Ye, Y. / Yang, H. / Shen, H.
History
DepositionMar 22, 2026Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Aug 12, 2026Provider: repository / Type: Initial release
Revision 1.0Aug 12, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Aug 12, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Aug 12, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Aug 12, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Aug 12, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Potassium voltage-gated channel subfamily KQT member 3
B: Green fluorescent protein,Potassium voltage-gated channel subfamily KQT member 2
C: Green fluorescent protein,Potassium voltage-gated channel subfamily KQT member 2
D: Green fluorescent protein,Potassium voltage-gated channel subfamily KQT member 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)331,61514
Polymers325,0054
Non-polymers6,61110
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Potassium voltage-gated channel subfamily KQT member 3 / KQT-like 3 / Potassium channel subunit alpha KvLQT3 / Voltage-gated potassium channel subunit Kv7.3


Mass: 71032.938 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KCNQ3 / Production host: Homo sapiens (human) / References: UniProt: O43525
#2: Protein Green fluorescent protein,Potassium voltage-gated channel subfamily KQT member 2 / KQT-like 2 / Neuroblastoma-specific potassium channel subunit alpha KvLQT2 / Voltage-gated ...KQT-like 2 / Neuroblastoma-specific potassium channel subunit alpha KvLQT2 / Voltage-gated potassium channel subunit Kv7.2


Mass: 84657.266 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aequorea victoria (jellyfish), (gene. exp.) Homo sapiens (human)
Gene: GFP, KCNQ2 / Production host: Homo sapiens (human) / References: UniProt: P42212, UniProt: O43526
#3: Chemical
ChemComp-A1E7E / ~{N}-(7-cyclopropyl-1-prop-2-ynyl-indazol-3-yl)-4-fluoranyl-benzamide


Mass: 333.359 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C20H16FN3O
#4: Chemical ChemComp-9PE / (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate / 3-SN-PHOSPHATIDYLETHANOLAMINE


Mass: 593.773 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C30H60NO8P / Feature type: SUBJECT OF INVESTIGATION / Comment: phospholipid*YM
#5: Chemical ChemComp-YJ0 / (2R)-2-{[(4-O-hexopyranosyl-beta-D-glucopyranosyl)oxy]methyl}-4-{[(25R)-5beta,14beta,17beta-spirostan-3beta-yl]oxy}butyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside


Mass: 1165.315 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C56H92O25
Has ligand of interestY
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: the human KCNQ2/KCNQ3 heterotetramer (3:1 stoichiometry)
Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1500 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameCategory
1cryoSPARCparticle selection
13PHENIX3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.07 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 15162 / Symmetry type: POINT
RefinementHighest resolution: 3.07 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0038609
ELECTRON MICROSCOPYf_angle_d0.711688
ELECTRON MICROSCOPYf_dihedral_angle_d14.2511398
ELECTRON MICROSCOPYf_chiral_restr0.041321
ELECTRON MICROSCOPYf_plane_restr0.0041350

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