GluRs come into focus.
Finally, a glimpse of a full-length tetrameric glutamate receptor.
The structure presented by Sobolevsky et al. is of one of the main glutamate-receptor subtypes, an AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid) receptor from the rat. It is made up of four GluA2 subunits (GluR2 in older nomenclature) that are identical in terms of amino-acid sequence, and it encompasses three structural/functional domains. Two of these domains are located on the external side of the cell membrane, and we have seen them individually before — the modulatory amino-terminal domain (ATD) and the ligand-binding domain (LBD) with its clam-shell-like arrangement. The third component is the transmembrane domain (TMD), which forms the ion channel, and this is our first view of it. In many ways the structure is comforting, because it consolidates and verifies much previous functional and structural work. But at the same time it is exhilarating, owing to the unexpected way in which these domains are intertwined and linked together.
Article here.