› 2ndj

Solution NMR

Structural Basis for KCNE3 and Estrogen Modulation of the KCNQ1 Channel

Released:
DOI: 10.2210/pdb2ndj/pdb
PDB entry 2ndj coloured by chain, ensemble of 10 models, front view.
PDB entry 2ndj coloured by chain, ensemble of 10 models, side view.
PDB entry 2ndj coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for KCNE3 modulation of potassium recycling in epithelia.
Kroncke BM, Van Horn WD, Smith J, Kang C, Welch RC, Song Y, Nannemann DP, Taylor KC, Sisco NJ, George AL, Meiler J, Vanoye CG, Sanders CR
Sci Adv 2 e1501228 (2016)
PMID: 27626070

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195364 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Potassium voltage-gated channel subfamily E member 3 Chain: A
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 12.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y6H6 (Residues: 1-103; Coverage: 100%)
Gene name: KCNE3
Sequence domains: Slow voltage-gated potassium channel

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 34%
Refinement method: DGSA-distance geometry simulated annealing, molecular dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Sexual Dimorphism in Colon Cancer.
Abancens et al. (2020)
10 more

1 mention without citation

Allosteric mechanism for KCNE1 modulation of KCNQ1 potassium channel activation.
Kuenze et al. (2020)