3o21

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o21 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o21 RCSB], [http://www.ebi.ac.uk/pdbsum/3o21 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o21 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o21 RCSB], [http://www.ebi.ac.uk/pdbsum/3o21 PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/GRIA3_RAT GRIA3_RAT]] Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. 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 (By similarity).
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 23:16, 24 December 2014

High resolution structure of GluA3 N-terminal domain (NTD)

3o21, resolution 2.20Å

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