Differential contribution by conserved glutamate residues to an ion-selectivity site in the L-type Ca2+ channel pore

FEBS Lett. 1993 Dec 6;335(2):265-9. doi: 10.1016/0014-5793(93)80743-e.

Abstract

In voltage-gated cation channels, it is thought that residues responsible for ion-selectivity are located within the pore-lining SS1-SS2 segments. In this study, we compared the ion permeation properties of mutant calcium channels in which highly conserved glutamate residues, located at analogous positions in the SS2 regions of all four motifs, were individually replaced. All of the mutants exhibited a loss of selectivity for divalent over monovalent cations. However, the permeation properties of the individual mutants varied in a position dependent manner. The results provide strong evidence that these glutamate residues, positioned at equivalent locations in the aligned sequences, play significantly different roles in forming the selectivity barrier of the calcium channel, and are probably arranged in an asymmetrical manner inside the ion-conducting pore.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Barium / metabolism
  • Binding Sites
  • Calcium Channels / chemistry
  • Calcium Channels / metabolism*
  • Conserved Sequence*
  • Glutamates / physiology*
  • Glutamic Acid
  • Humans
  • Molecular Sequence Data
  • Mutation
  • Sequence Homology, Amino Acid
  • Sodium / metabolism
  • Structure-Activity Relationship

Substances

  • Calcium Channels
  • Glutamates
  • Barium
  • Glutamic Acid
  • Sodium