scholarly journals Crystal structure of a heterotetrameric NMDA receptor ion channel

Science ◽  
2014 ◽  
Vol 344 (6187) ◽  
pp. 992-997 ◽  
Author(s):  
E. Karakas ◽  
H. Furukawa
Keyword(s):  
Crystal Structure ◽  
Nmda Receptor ◽  
Ion Channel

Endogenous ion channel complexes: the NMDA receptor

2011 ◽  
Vol 39 (4) ◽  
pp. 1113-1113
Author(s):  
René Frank
Keyword(s):  
Nmda Receptor ◽  
Ion Channel

Mechanism of ligand binding – PDZ domain taken as example

2017 ◽  
Vol 13 (4) ◽  
Author(s):  
Dawid Dułak ◽  
Mateusz Banach ◽  
Zdzisław Wiśniowski ◽  
Leszek Konieczny ◽  
Irena Roterman
Keyword(s):  
Crystal Structure ◽  
Ligand Binding ◽  
Ion Channel ◽  
Pdz Domain ◽  
Traditional Model ◽  
Beta Sheet ◽  
Hydrophobic Core ◽  
Beta Strand ◽  
Model Based ◽  
Specific Ligand

AbstractThe mechanism of specific ligand binding by proteins is discussed using the PDZ domain complexing the pentapeptide. This process is critical for clustering the membrane ion channel. The traditional model based on the Beta-sheet extension by complexed pentapeptide is interpreted as a hydrophobic core extension supported by additional Beta-strand generated by complexed pentapeptide. The explanation is based on the fuzzy oil drop model applied to the crystal structure of PDZ-pentapeptide.

Endogenous ion channel complexes: the NMDA receptor

2011 ◽  
Vol 39 (3) ◽  
pp. 707-718 ◽  
Author(s):  
René A.W. Frank
Keyword(s):  
Nmda Receptor ◽  
Ion Channel ◽  
Present Article ◽  
Neuronal Excitability ◽  
Structure And Function ◽  
Current Understanding ◽  
Ionotropic Receptors ◽  
Receptor Complexes ◽  
Aspartate Receptor ◽  
And Function

Ionotropic receptors, including the NMDAR (N-methyl-D-aspartate receptor) mediate fast neurotransmission, neurodevelopment, neuronal excitability and learning. In the present article, the structure and function of the NMDAR is reviewed with the aim to condense our current understanding and highlight frontiers where important questions regarding the biology of this receptor remain unanswered. In the second part of the present review, new biochemical and genetic approaches for the investigation of ion channel receptor complexes will be discussed.

scholarly journals Crystal Structure and Pharmacological Characterization of a NovelN-Methyl-d-aspartate (NMDA) Receptor Antagonist at the GluN1 Glycine Binding Site

2013 ◽  
Vol 288 (46) ◽  
pp. 33124-33135 ◽  
Author(s):  
Trine Kvist ◽  
Thomas Bielefeldt Steffensen ◽  
Jeremy R. Greenwood ◽  
Fatemeh Mehrzad Tabrizi ◽  
Kasper B. Hansen ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nmda Receptor ◽  
Receptor Antagonist ◽  
Binding Site ◽  
Nmda Receptor Antagonist ◽  
Pharmacological Characterization
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