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Solution NMR

Structural Basis for KCNE3 and Estrogen Modulation of the KCNQ1 Channel

Released:
DOI: 10.2210/pdb2ndj/pdb
PDB 2ndj coloured by chain and viewed from the front.
PDB 2ndj coloured by chain and viewed from the side.
PDB 2ndj coloured by chain and viewed from the top.
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
OpenAccess logo 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)
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

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 40%
Refinement method: DGSA-distance geometry simulated annealing, molecular dynamics
Chemical shifts: BMR16621  
Expression system: Escherichia coli BL21(DE3)

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Citations

8 review citations

Sex disparities in cystic fibrosis: review on the effect of female sex hormones on lung pathophysiology and outcomes.
Lam et al. (2021)
7 more