Self-assembly of the isolated KCNQ2 subunit interaction domain

FEBS Lett. 2007 Apr 17;581(8):1594-8. doi: 10.1016/j.febslet.2007.03.024. Epub 2007 Mar 16.


Mutations in the KCNQ2 gene cause myokymia and neonatal epilepsy, indicating that this K(+) channel regulates the excitability of lower motoneurons and CNS neurons. Little is known about the parameters that direct the assembly of this multimeric molecule and other KCNQ subunits. Here, we show that the carboxy-terminal subunit interaction domain of KCNQ2 autonomously folds and assembles into tetramers. This domain contains a bipartite coiled-coil motif. Whereas structural integrity of the second coiled-coil motif is crucial for tetramer formation, that of the first motif is less important. These data suggest a crucial role of coiled-coil motifs in tetrameric KCNQ channel assembly.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Humans
  • KCNQ2 Potassium Channel / chemistry*
  • KCNQ2 Potassium Channel / genetics
  • Molecular Sequence Data
  • Protein Folding
  • Protein Structure, Tertiary / genetics


  • KCNQ2 Potassium Channel