› 2lqc

Solution NMR

NMR solution structure of a Ca2+-Calmodulin with a binding motif (NSCaTE) peptide from the N-terminal cytoplasmic domain of the L-type Voltage-Cated Calcium Channel alpha1C subunit

Released:
DOI: 10.2210/pdb2lqc/pdb
PDB entry 2lqc coloured by chain, ensemble of 20 models, front view.
PDB entry 2lqc coloured by chain, ensemble of 20 models, side view.
PDB entry 2lqc coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the regulation of L-type voltage-gated calcium channels: interactions between the N-terminal cytoplasmic domain and Ca(2+)-calmodulin.
Liu Z, Vogel HJ
Front Mol Neurosci 5 38 (2012)
PMID: 22518098

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143947 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Calmodulin-1 Chain: A
Molecule details ›
Chain: A
Length: 77 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DP23 (Residues: 2-78; Coverage: 52%)
Gene names: CALM, CALM1, CAM, CAM1
Sequence domains: EF-hand domain pair
Voltage-dependent L-type calcium channel subunit alpha-1C Chain: B
Molecule details ›
Chain: B
Length: 24 amino acids
Theoretical weight: 2.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13936 (Residues: 47-68; Coverage: 1%)
Gene names: CACH2, CACN2, CACNA1C, CACNL1A1, CCHL1A1

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 77%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Neuronal voltage-gated calcium channels: structure, function, and dysfunction.
Simms et al. (2014)
10 more

7 mentions without citation

Calmodulin regulation (calmodulation) of voltage-gated calcium channels.
Ben-Johny et al. (2014)
6 more