› 2l0w

Solution NMR

Solution NMR structure of the N-terminal PAS domain of HERG potassium channel

Released:
DOI: 10.2210/pdb2l0w/pdb
PDB entry 2l0w coloured by chain, ensemble of 20 models, front view.
PDB entry 2l0w coloured by chain, ensemble of 20 models, side view.
PDB entry 2l0w coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The N-terminal tail of hERG contains an amphipathic α-helix that regulates channel deactivation.
Ng CA, Hunter MJ, Perry MD, Mobli M, Ke Y, Kuchel PW, King GF, Stock D, Vandenberg JI
PLoS One 6 e16191 (2011)
PMID: 21249148

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171399 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium voltage-gated channel subfamily H member 2 Chain: A
Molecule details ›
Chain: A
Length: 138 amino acids
Theoretical weight: 15.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12809 (Residues: 1-135; Coverage: 12%)
Gene names: ERG, ERG1, HERG, KCNH2
Sequence domains: PAS domain
Structure domains: PAS domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 85%
Refinement method: DGSA-distance geometry simulated annealing, Generalised Born Energy Minimization, GENERALISED BORN ENERGY MINIMIZATION WITH NMR RESTRAINTS
Expression system: Escherichia coli

Quick links

Citations

11 review citations

hERG K(+) channels: structure, function, and clinical significance.
Vandenberg et al. (2012)
10 more

8 mentions without citation

HERG potassium channel regulation by the N-terminal eag domain.
Gustina et al. (2012)
7 more