Figure 1.
FIGURE 1. Structure of ionotropic glutamate receptors and
ligands. A, an individual subunit is highlighted on the left and
is formed by a single polypeptide chain beginning with the
N-terminal LIVBP (leucine-isoleucine-valine-binding
protein)-like domain, which is followed by S1 forming the
majority of domain 1 (D1) of the ligand binding core (red). The
amino acid chain then transverses domain 2 (D2) of the ligand
binding core and forms M1, the P-loop, and M2. Subsequently, the
rest of domain 2 (D2, blue) is formed by S2, ending up in the
last transmembrane -helix (M3) and the
intracellular C-terminal domain. The flip/flop region lies on
the back, primarily of the D1. Scissors indicate where the
corresponding receptor has been cleaved during construction of
the GluR2-S1S2J construct. B, structures of selected AMPA
receptor agonists.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2005,
280,
35469-35476)
copyright 2005.
-helix (M3) and the
intracellular C-terminal domain. The flip/flop region lies on
the back, primarily of the D1. Scissors indicate where the
corresponding receptor has been cleaved during construction of
the GluR2-S1S2J construct. B, structures of selected AMPA
receptor agonists.