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Crystal Structure of glutamate receptor GluA1 Amino Terminal Domain
Structural highlights
FunctionGRIA1_RAT Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate.[1] [2] Publication Abstract from PubMedThe alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) subfamily of ionotropic glutamate receptors (iGluRs) is essential for fast excitatory neurotransmission in the central nervous system. The malfunction of AMPARs has been implicated in many neurological diseases including Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis. The active channels of AMPARs and other iGluR subfamilies are tetramers formed exclusively by assembly of subunits within the same subfamily. It has been proposed that the assembly process is controlled mainly by the extracellular amino-terminal domain (ATD) of iGluR. In addition, ATD has also been implicated in synaptogenesis, iGluR trafficking, and trans-synaptic signaling, through unknown mechanisms. We report here a 2.5 A resolution crystal structure of the ATD of GluA1. Comparative analyses of the structure of GluA1-ATD and other subunits sheds light on our understanding of how ATD drives subfamily-specific assembly of AMPARs. In addition, analysis of the crystal lattice of GluA1-ATD suggests a novel mechanism by which the ATD might participate in inter-tetramer AMPAR clustering, as well as in trans-synaptic protein-protein interactions. Crystal structure of the glutamate receptor GluA1 amino-terminal domain.,Yao G, Zong Y, Gu S, Zhou J, Xu H, Mathews II, Jin R Biochem J. 2011 Jun 6. PMID:21639859[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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