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Mg2+ binds Grin1:Grin2 NMDA receptors
Stable Identifier
R-RNO-9614228
Type
Reaction [binding]
Species
Rattus norvegicus
Compartment
plasma membrane
,
extracellular region
ReviewStatus
5/5
General
SBML
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BioPAX
Level 2
Level 3
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PDF
SVG
|
PNG
Low
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High
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SBGN
The pore of the NMDA receptor is blocked by binding of Mg2+ ions. Studies of recombinant rat NMDA receptors have shown that the strength of the Mg2+ block and the kinetics of unblocking depend on the subunit composition of the NMDA receptor, as both the GluN1 (Grin1, Nr1) subunit and GluN2 (Grin2, Nr2) subunits (GluN2A, GluN2B, GluN2c and GluN2D - officially named Grin2a, Grin2b, Grin2c and Grin2d, respectively) interact with Mg2+, but GluN2 subunits differ in their affinity for Mg2+ and sensitivity to membrane depolarization (Siegler Retchless et al. 2012, Clarke et al. 2013).
Literature References
PubMed ID
Title
Journal
Year
23447622
Mechanistic and structural determinants of NMDA receptor voltage-dependent gating and slow Mg2+ unblock
Johnson, JW
,
Glasgow, NG
,
Clarke, RJ
J. Neurosci.
2013
22246434
A single GluN2 subunit residue controls NMDA receptor channel properties via intersubunit interaction
Johnson, JW
,
Gao, W
,
Siegler Retchless, B
Nat. Neurosci.
2012
Participants
Input
Grin1:Grin2 di-heterotetramers [plasma membrane]
(Rattus norvegicus)
Mg2+ [extracellular region]
Output
Grin1:Grin2 di-heterotetramers:Mg2+ [plasma membrane]
(Rattus norvegicus)
Orthologous Events
Mg2+ binds GRIN1:GRIN2 NMDA receptors (Homo sapiens)
Authored
Orlic-Milacic, M (2018-07-24)
Reviewed
Gillespie, ME (2018-07-28)
D'Eustachio, P (2018-07-27)
Hansen, KB (2018-11-02)
Yi, F (2018-11-02)
Created
Orlic-Milacic, M (2018-07-24)
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