Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors

Erkan Karakas, Noriko Simorowski and Hiro Furukawa ()
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Erkan Karakas: Cold Spring Harbor Laboratory, WM Keck Structural Biology Laboratory
Noriko Simorowski: Cold Spring Harbor Laboratory, WM Keck Structural Biology Laboratory
Hiro Furukawa: Cold Spring Harbor Laboratory, WM Keck Structural Biology Laboratory

Nature, 2011, vol. 475, issue 7355, 249-253

Abstract: Targeting NMDA receptors Ifenprodil, a phenylethanolamine first developed as an adrenergic antagonist and now widely used as an antihypertensive, also has a neuroprotective effect through receptors. A study of this interaction shows that the NMDA receptor subunits GluN1 and GluN2B form heterodimers that bind ifenprodil at the GluN1/GluN2B interface. Conformational mobility in the GluN2B amino-terminal domain is essential for ifenprodil-mediated inhibition of the NMDA receptors. These findings may be relevant to the design of therapeutics to target specific NMDA receptor subtypes for use in neurological disorders.

Date: 2011
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DOI: 10.1038/nature10180

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