[HTML][HTML] Arginine 445 controls the coupling between glutamate and cations in the neuronal transporter EAAC-1
L Borre, BI Kanner - Journal of Biological Chemistry, 2004 - ASBMB
The substrate-binding sites in membrane transporters are alternately accessible from either
side of the membrane, but the molecular basis of how this alternate opening of internal and
external gates is achieved is largely unknown. Here we present data indicating that, in the
neuronal electrogenic sodium-and potassium-coupled glutamate transporter EAAC-1, the
substrate-binding site and one of the gates, or a residue controlling the gating process, are
in close physical proximity. Arginine 445, located only two residues away from a residue …
side of the membrane, but the molecular basis of how this alternate opening of internal and
external gates is achieved is largely unknown. Here we present data indicating that, in the
neuronal electrogenic sodium-and potassium-coupled glutamate transporter EAAC-1, the
substrate-binding site and one of the gates, or a residue controlling the gating process, are
in close physical proximity. Arginine 445, located only two residues away from a residue …