Abstract：
:Fast desensitization is an important regulatory mechanism of neuronal NMDA receptor function. Only recombinant NMDA receptors composed of NR1/NR2A exhibit a fast component of desensitization similar to neuronal NMDA receptors. Here we report that the fast desensitization of NR1/NR2A receptors is caused by ambient zinc, and that a positive allosteric interaction occurs between the extracellular zinc-binding site located in the amino terminal domain and the glutamate-binding domain of NR2A. The relaxation of macroscopic currents reflects a shift to a new equilibrium due to increased zinc affinity after binding of glutamate. We also show a similar interaction between the ifenprodil binding site and the glutamate binding site of NR1/NR2B receptors. These data raise the possibility that there is an allosteric interaction between the amino terminal domain and the ligand-binding domain of other glutamate receptors. Our findings may provide insight into how zinc and other extracellular modulators regulate NMDA receptor function.
journal_name
Nat Neuroscijournal_title
Nature neuroscienceauthors
Zheng F,Erreger K,Low CM,Banke T,Lee CJ,Conn PJ,Traynelis SFdoi
10.1038/nn0901-894subject
Has Abstractpub_date
2001-09-01 00:00:00pages
894-901issue
9eissn
1097-6256issn
1546-1726pii
nn0901-894journal_volume
4pub_type
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