The glutamate activated cationic channels are made of four homologous subunits. Each subunit contains an extra-cellular amino-terminal domain similar to the bacterial leucine, isoleucine, valine binding protein (LIVBP), followed by half of the agonist binding core, two transmembrane domains separated by a "P-loop", the second half of the agonist-binding core (the agonist binding core is similar to the bacterial lysine, arginine, ornithine binding protein (LAOBP)) and a third transmembrane segment. The cytoplasmic tail has a variable length.

Available Sequences

108 entries:

• ordered by LGICdb ID

• ordered by species

Phylogenetic Studies

Bibliography

Mayer M.L., Armstrong N. (2004). Structure and function of glutamate receptor ion channels. Annu Rev Physiol 66: 161-81.

Wollmuth L.P., Sobolevsky A.I. (2004). Structure and gating of the glutamate receptor ion channel. Trends Neurosci 27: 321-328.

Chiu J., DeSalle R., Lam H.-M., Maisel L., Coruzzi G. (1999). Molecular evolution of glutamate receptors: A primitive signaling mechanism that existed before plants and animals diverged. Mol Biol Evol 16: 826-838.

Dingledine R., Borges K., Bowie D., Traynelis S.F. (1999). The glutamate receptor ion channels. Pharmacol Rev 51: 7-61.

Hollman M. (1999). Ionotropic glutamate receptors in the CNS. Handbook of experimental pharmacology vol 141: 1-98.

Last modification: Wed Nov 24 10:59:05 GMT 2004 | Nicolas Le Novère