Glutamate receptors structure

Constantino, G., Macchiarulo, A., Pellicciari, R. Modeling of amino-terminal domains of group I metabotropic glutamate receptors structural motifs affecting ligand selectivity, J. Med. Chem. 1999, 42, 5390-5401. 

Pin JP, Acher F. 2002. The metabotropic glutamate receptors Structure, activation mechanism and pharmacology. Curr... 

Kew JN, Kemp JA. 2005. Ionotropic and metabotropic glutamate receptor structure and pharmacology. Psychopharmacology (Berl) 179 4-29. 

Pellicciari R, Costantino G, Marinozzi M, Macchiarulo A, Camaioni E, et al. 2001. Metabotropic glutamate receptors Structure and new subtype-selective ligands. Farmaco 56 91-94. 

Pirr JP, Duvoisirr R (1995) The metabotropic glutamate receptors Structure and furrctiorrs. Neurophaimacology 34 1—26. 

Pin J-P, Duvoisin R (1995) Review neurotransmitter receptors I. The metabotropic glutamate receptors structure and functions. Neuropharmacology 34 1 -26. 

Kunishima N, Shimada Y, Tsuji Y et al (2000) Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor. Nature 407 971-977... 

Structures of spider toxins that antagonise insect muscle glutamate receptors (and glutamate receptors of other animals)... 

Most of the G-protein-coupled receptors are homologous with rhodopsin however, other quantitatively minor families as well as some individual receptors do not share any of the structural features common to the rhodopsin family (Figure 2.3). The most dominant of these are the glucagon/VIP/caldtonin receptor family, or family B (which has approximately 65 members), and the metabotropic glutamate receptor family, or family C (which has approximately 15 members), as well as the frizzled/smoothened family of receptors. Thus, the only structural feature that all G-protein-coupled receptors have in common is the seven-transmembrane helical bundle. Nevertheless, most non-rhodopsin-like receptors do have certain minor structural features in common with the rhodopsin-like receptors — for example, a disulfide bridge between the top of TM-III and the middle of extracellular loop-3, and a cluster of basic residues located just below TM-VI. 

Structural and functional evidence clearly demonstrates that family C receptors function as dimers, either as homodimers or as heterodimers. The metabotropic glutamate receptors and the calcium sensors, as discussed in Section 2.6.1, are found as covalently connected dimers in which there is a disulfide bridge between a Cys residue located in a loop in the N-terminal extracellular domain of each monomer. This disulfide bridge apparently serves only to hold the monomers in close proximity, as the loop is so unstructured that it does not resolve in the x-ray structure. 

For family C receptors, the importance of and structural basis for interaction with intracellular adaptor or scaffolding proteins have been characterized in great detail, just as the issue of dimer formation is rather clear for these receptors. The main family of adaptor proteins, which ensures the cellular targeting and correct signaling function for the metabotropic glutamate receptors, appear... 

Kunishima, N., Shimada, Y., Tsuji, Y., Sato, T., Yamamoto, M., Kumasaka, T., Nakanishi, S., Jingami, H., and Morikawa, K., Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor, Nature, 407(6807), 971-977, 2000. 

Armstrong, N. and Gouaux, E., Mechanisms for activation and antagonism of the AMPA-sensitive glutamate receptor crystal structures of the GluR2 ligand binding core, Neuron, 28, 165-181, 2000. 

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