Structural highlights
9wqn is a 6 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
|
| Method: | Electron Microscopy, Resolution 3.7Å |
| Ligands: | A1EX5, CL, CLR, GGL, NAG |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Disease
GRM1_HUMAN Autosomal recessive congenital cerebellar ataxia due to MGLUR1 deficiency. The disease is caused by mutations affecting the gene represented in this entry.[1]
Function
GRM1_HUMAN G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum.[2]
References
- ↑ Guergueltcheva V, Azmanov DN, Angelicheva D, Smith KR, Chamova T, Florez L, Bynevelt M, Nguyen T, Cherninkova S, Bojinova V, Kaprelyan A, Angelova L, Morar B, Chandler D, Kaneva R, Bahlo M, Tournev I, Kalaydjieva L. Autosomal-recessive congenital cerebellar ataxia is caused by mutations in metabotropic glutamate receptor 1. Am J Hum Genet. 2012 Sep 7;91(3):553-64. doi: 10.1016/j.ajhg.2012.07.019. Epub, 2012 Aug 16. PMID:22901947 doi:https://dx.doi.org/10.1016/j.ajhg.2012.07.019
- ↑ Desai MA, Burnett JP, Mayne NG, Schoepp DD. Cloning and expression of a human metabotropic glutamate receptor 1 alpha: enhanced coupling on co-transfection with a glutamate transporter. Mol Pharmacol. 1995 Oct;48(4):648-57. PMID:7476890
