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› 7k48

Electron Microscopy
3.6Å resolution

Structure of NavAb/Nav1.7-VS2A chimera trapped in the resting state by tarantula toxin m3-Huwentoxin-IV

Released:
DOI: 10.2210/pdb7k48/pdb
PDB entry 7k48 coloured by chain, front view.
PDB entry 7k48 coloured by chain, side view.
PDB entry 7k48 coloured by chain, top view.
Source organisms:
Primary publication:
Structural Basis for High-Affinity Trapping of the NaV1.7 Channel in Its Resting State by Tarantula Toxin.
Wisedchaisri G, Tonggu L, Gamal El-Din TM, McCord E, Zheng N, Catterall WA
Mol Cell 81 38-48.e4 (2021)
PMID: 33232657
Related structures: EMD-22661

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108626 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ion transport domain-containing protein; Maltose/maltodextrin-binding periplasmic protein; Sodium channel protein type 9 subunit alpha Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 611 amino acids
Theoretical weight: 68.52 KDa
Source organisms: Expression system: Trichoplusia ni
UniProt:
  • Canonical: P0AEX9 (Residues: 27-392; Coverage: 99%)
  • Canonical: A8EVM5 (Residues: 1-18, 60-84, 106-239; Coverage: 66%)
  • Canonical: Q15858 (Residues: 751-790, 817-841; Coverage: 3%)
Gene names: Abu_1752, JW3994, NENA, SCN9A, b4034, malE
Sequence domains:
Huwentoxin-IV Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 35 amino acids
Theoretical weight: 4 KDa
Source organism: Cyriopagopus schmidti
Expression system: Not provided
UniProt:
  • Canonical: P83303 (Residues: 53-87; Coverage: 54%)
Sequence domains: Ion channel inhibitory toxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 3.6Å
Relevant EMDB volumes: EMD-22661
Expression systems:
  • Trichoplusia ni
  • Not provided

Quick links

Citations

3 review citations

Druggability of Voltage-Gated Sodium Channels-Exploring Old and New Drug Receptor Sites.
Wisedchaisri et al. (2022)
2 more

10 mentions without citation

Structural Advances in Voltage-Gated Sodium Channels.
Jiang et al. (2022)
9 more