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]
Collections | ANU Research Publications |
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Date published: | 2000 |
Type: | Journal article |
URI: | http://hdl.handle.net/1885/91117 |
Source: | Biophysical Journal |
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01_Buck_NMDA_Channel_Gating_is_2000.pdf | 173.14 kB | Adobe PDF | Request a copy |
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