|Entry||Database: PDB / ID: 6j8e|
|Title||Human Nav1.2-beta2-KIIIA ternary complex|
|Keywords||MEMBRANE PROTEIN/TOXIN / transmembrane protein / MEMBRANE PROTEIN / MEMBRANE PROTEIN-TOXIN complex|
|Function / homology||Immunoglobulin-like fold / Voltage-dependent channel domain superfamily / Voltage gated sodium channel, alpha subunit / Immunoglobulin subtype / Ion transport domain / IQ motif, EF-hand binding site / Immunoglobulin-like domain / Sodium ion transport-associated / Immunoglobulin V-set domain / Voltage-gated Na+ ion channel, cytoplasmic domain ...Immunoglobulin-like fold / Voltage-dependent channel domain superfamily / Voltage gated sodium channel, alpha subunit / Immunoglobulin subtype / Ion transport domain / IQ motif, EF-hand binding site / Immunoglobulin-like domain / Sodium ion transport-associated / Immunoglobulin V-set domain / Voltage-gated Na+ ion channel, cytoplasmic domain / Sodium channel subunit beta-2 / Myelin P0 protein-related / Immunoglobulin-like domain superfamily / Ion transport protein / Sodium ion transport-associated / Immunoglobulin V-set domain / Cytoplasmic domain of voltage-gated Na+ ion channel / IQ motif profile. / Ig-like domain profile. / Interaction between L1 and Ankyrins / Phase 0 - rapid depolarisation / response to pyrethroid / regulation of atrial cardiac muscle cell membrane depolarization / voltage-gated sodium channel activity involved in cardiac muscle cell action potential / sodium channel complex / regulation of sodium ion transmembrane transporter activity / cardiac muscle cell action potential involved in contraction / membrane depolarization during cardiac muscle cell action potential / voltage-gated sodium channel complex / membrane depolarization during action potential / paranode region of axon / node of Ranvier / voltage-gated sodium channel activity / neuronal action potential / intrinsic apoptotic signaling pathway in response to osmotic stress / regulation of heart rate by cardiac conduction / sodium ion transmembrane transport / sodium ion transport / voltage-gated ion channel activity / myelination / intrinsic component of plasma membrane / intercalated disc / regulation of ion transmembrane transport / T-tubule / cardiac muscle contraction / sodium channel regulator activity / integral component of presynaptic membrane / neuron apoptotic process / nervous system development / chemical synaptic transmission / toxin activity / glutamatergic synapse / axon / integral component of plasma membrane / extracellular region / plasma membrane / Sodium channel subunit beta-2 / Mu-conotoxin KIIIB / Sodium channel protein type 2 subunit alpha|
Function and homology information
|Specimen source||Homo sapiens (human)|
Conus kinoshitai (invertebrata)
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / 3 Å resolution|
|Authors||Pan, X. / Li, Z. / Huang, X. / Huang, G. / Yan, N.|
|Citation||Journal: Science / Year: 2019|
Title: Molecular basis for pore blockade of human Na channel Na1.2 by the μ-conotoxin KIIIA.
Authors: Xiaojing Pan / Zhangqiang Li / Xiaoshuang Huang / Gaoxingyu Huang / Shuai Gao / Huaizong Shen / Lei Liu / Jianlin Lei / Nieng Yan
Abstract: The voltage-gated sodium channel Na1.2 is responsible for the initiation and propagation of action potentials in the central nervous system. We report the cryo-electron microscopy structure of human ...The voltage-gated sodium channel Na1.2 is responsible for the initiation and propagation of action potentials in the central nervous system. We report the cryo-electron microscopy structure of human Na1.2 bound to a peptidic pore blocker, the μ-conotoxin KIIIA, in the presence of an auxiliary subunit β2 to an overall resolution of 3.0 Å. The immunoglobulin (Ig) domain of β2 interacts with the shoulder of the pore domain through a disulfide bond. The 16-residue KIIIA interacts with the extracellular segments in repeats I to III, placing Lys7 at the entrance to the selectivity filter. Many interacting residues are specific to Na1.2, revealing a molecular basis for KIIIA specificity. The structure establishes a framework for rational design of subtype-specific blockers for Na channels.
SummaryFull reportAbout validation report
|Date||Deposition: Jan 18, 2019 / Release: Feb 27, 2019|
|Structure viewer||Molecule: |
Downloads & links
C: Sodium channel subunit beta-2
A: Sodium channel protein type 2 subunit alpha
D: Mu-conotoxin KIIIA
-Sodium channel ... , 2 types, 2 molecules C
|#1: Protein/peptide|| |
Mass: 14267.261 Da / Num. of mol.: 1 / Source: (gene. exp.) Homo sapiens (human) / Gene: SCN2B, UNQ326/PRO386 / Production host: Homo sapiens (human) / References: UniProt: O60939
|#2: Protein/peptide|| |
Mass: 232800.172 Da / Num. of mol.: 1 / Source: (gene. exp.) Homo sapiens (human) / Gene: SCN2A, NAC2, SCN2A1, SCN2A2 / Production host: Homo sapiens (human) / References: UniProt: Q99250
-Protein/peptide , 1 types, 1 molecules D
|#3: Protein/peptide|| |
Mass: 1895.220 Da / Num. of mol.: 1 / Source: (synth.) Conus kinoshitai (invertebrata) / References: UniProt: P0C195
-Non-polymers , 4 types, 10 molecules
|#5: Chemical|| ChemComp-BMA / ||#6: Chemical|| ChemComp-9Z9 / (||#7: Chemical|| ChemComp-NA / |
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / Reconstruction method: single particle reconstruction|
|Molecular weight||Value: 252 kDa/nm / Experimental value: YES|
|Source (recombinant)||Organism: Homo sapiens (human)|
|Buffer solution||pH: 5.9|
|Specimen||Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Microscope model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Electron dose: 48 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 QUANTUM (4k x 4k)|
|CTF correction||Type: PHASE FLIPPING ONLY|
|3D reconstruction||Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Number of particles: 200275 / Symmetry type: POINT|
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