› 6but

Solution NMR

Solution structure of full-length apo mammalian calmodulin bound to the IQ motif of the human voltage-gated sodium channel NaV1.2

Released:
DOI: 10.2210/pdb6but/pdb
PDB entry 6but coloured by chain, ensemble of 20 models, front view.
PDB entry 6but coloured by chain, ensemble of 20 models, side view.
PDB entry 6but coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
NaV1.2 EFL domain allosterically enhances Ca2+ binding to sites I and II of WT and pathogenic calmodulin mutants bound to the channel CTD.
Mahling R, Hovey L, Isbell HM, Marx DC, Miller MS, Kilpatrick AM, Weaver LD, Yoder JB, Kim EH, Andresen CNJ, Li S, Shea MA
Structure 29 1339-1356.e7 (2021)
PMID: 33770503

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143957 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Calmodulin-1 Chain: A
Molecule details ›
Chain: A
Length: 148 amino acids
Theoretical weight: 16.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DP23 (Residues: 2-149; Coverage: 99%)
Gene names: CALM, CALM1, CAM, CAM1
Sequence domains: EF-hand domain pair
Sodium channel protein type 2 subunit alpha Chain: B
Molecule details ›
Chain: B
Length: 31 amino acids
Theoretical weight: 3.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99250 (Residues: 1901-1927; Coverage: 1%)
Gene names: HBA, NAC2, SCN2A, SCN2A1, SCN2A2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 87%
Refinement method: molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Calmodulin Interactions with Voltage-Gated Sodium Channels.
Wu et al. (2021)
1 other article

5 mentions without citation

Structural basis of cytoplasmic NaV1.5 and NaV1.4 regulation.
Nathan et al. (2021)
4 more