The structure of glutamate transporters shows channel-like features.
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.
Slotboom
D J
DJ
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN, Haren, The Netherlands.
Konings
W N
WN
Lolkema
J S
JS
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000378:metabolism; D027322:Amino Acid Transport System X-AG; D000818:Animals; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D009474:Neurons / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D020539:Sequence Analysis, Protein; D009435:Synaptic Transmission / Q000502:physiology
D018528:ATP-Binding Cassette Transporters; D027322:Amino Acid Transport System X-AG; D008565:Membrane Proteins