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NMDA Channel Gating is Influenced by a Tryptophan Residue in the M2 Domain but Calcium Permeation Is Not Altered

Buck, Damian; Howitt, Susan; Clements, John D

Description

N-Methyl-D-aspartate (NMDA) receptors are susceptible to open-channel block by dizolcipine (MK-801), ketamine and Mg2+ and are permeable to Ca2+. It is thought that a tryptophan residue in the second membrane-associated domain (M2) may form part of the binding site for open-channel blockers and contribute to Ca2+ permeability. We tested this hypothesis using recombinant wild-type and mutant NMDA receptors expressed in HEK-293 cells. The tryptophan was mutated to a leucine (W-5L) in both the...[Show more]

CollectionsANU Research Publications
Date published: 2000
Type: Journal article
URI: http://hdl.handle.net/1885/91117
Source: Biophysical Journal

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