Swapping of transmembrane domains in the epithelial calcium channel TRPV6

Sci Rep. 2017 Sep 6;7(1):10669. doi: 10.1038/s41598-017-10993-9.

Abstract

Tetrameric ion channels have either swapped or non-swapped arrangements of the S1-S4 and pore domains. Here we show that mutations in the transmembrane domain of TRPV6 can result in conversion from a domain-swapped to non-swapped fold. These results reveal structural determinants of domain swapping and raise the possibility that a single ion channel subtype can fold into either arrangement in vivo, affecting its function in normal or disease states.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Calcium / metabolism
  • Calcium Channels / chemistry*
  • Calcium Channels / genetics*
  • Calcium Channels / metabolism
  • Genes, Reporter
  • HEK293 Cells
  • Humans
  • Ligands
  • Models, Molecular
  • Molecular Conformation
  • Mutation
  • Protein Interaction Domains and Motifs*
  • Quantitative Structure-Activity Relationship
  • TRPV Cation Channels / chemistry*
  • TRPV Cation Channels / genetics*
  • TRPV Cation Channels / metabolism

Substances

  • Calcium Channels
  • Ligands
  • TRPV Cation Channels
  • TRPV6 protein, human
  • Calcium