The structure of glutamate transporters shows channel-like features

DJ Slotboom, WN Konings, JS Lolkema*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

29 Citations (Scopus)
223 Downloads (Pure)

Abstract

Neuronal and glial glutamate transporters remove the excitatory neurotransmitter glutamate from the synaptic cleft and thus prevent neurotoxicity, The proteins belong to a large family of secondary transporters, which includes transporters from a variety of bacterial, archaeal and eukaryotic organisms. The transporters consist of eight membrane-spanning alpha -helices and two pore-loop structures, which are unique among secondary transporters but may resemble pore-loops found in ion channels, Another distinctive structural feature is the presence of a highly amphipathic membrane-spanning alpha -helix that provides a hydrophilic path through the membrane. The unusual structural features of the transporters are discussed in relation to their function. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

Original languageEnglish
Pages (from-to)183-186
Number of pages4
JournalFEBS Letters
Volume492
Issue number3
DOIs
Publication statusPublished - 16-Mar-2001

Keywords

  • glutamate transporter
  • neurotransmission
  • channel
  • pore-loop
  • REENTRANT LOOP
  • SUBSTRATE
  • GLT-1
  • ACCESSIBILITY
  • TOPOLOGY
  • FAMILY
  • SELECTIVITY
  • SIMILARITY
  • PROTEINS
  • REVEALS

Cite this