9jvv
From Proteopedia
Overall structure of human EAAT2 in the substrate-free state
Structural highlights
DiseaseEAA2_HUMAN Non-specific early-onset epileptic encephalopathy. The disease is caused by variants affecting the gene represented in this entry. FunctionEAA2_HUMAN Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate (PubMed:14506254, PubMed:15265858, PubMed:26690923, PubMed:7521911). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion (PubMed:14506254). Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (PubMed:14506254). Essential for the rapid removal of released glutamate from the synaptic cleft, and for terminating the postsynaptic action of glutamate (By similarity).[UniProtKB:P43006][1] [2] [3] References
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Categories: Homo sapiens | Large Structures | Huang J | Shi Y | Xia LY | Zhang YY | Zhou Q