3q41: Difference between revisions
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{{STRUCTURE_3q41| PDB=3q41 | SCENE= }} | {{STRUCTURE_3q41| PDB=3q41 | SCENE= }} | ||
===Crystal structure of the GluN1 N-terminal domain (NTD)=== | ===Crystal structure of the GluN1 N-terminal domain (NTD)=== | ||
{{ABSTRACT_PUBMED_21389213}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/NMDZ1_RAT NMDZ1_RAT]] NMDA receptor subtype of glutamate-gated ion channels possesses high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. Plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors.<ref>PMID:15996549</ref> | |||
==About this Structure== | ==About this Structure== | ||
| Line 22: | Line 10: | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:021389213</ref><references group="xtra"/><references/> | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Blain, K Y.]] | [[Category: Blain, K Y.]] | ||
| Line 30: | Line 18: | ||
[[Category: Maruo, T.]] | [[Category: Maruo, T.]] | ||
[[Category: Nakagawa, T.]] | [[Category: Nakagawa, T.]] | ||
[[Category: Glun1]] | |||
[[Category: Glycosylation]] | |||
[[Category: Ion channel]] | |||
[[Category: Nmda]] | |||
[[Category: Ntd]] | |||
[[Category: Transport protein]] | |||
Revision as of 08:09, 8 May 2013
Crystal structure of the GluN1 N-terminal domain (NTD)
Template:ABSTRACT PUBMED 21389213
Function
[NMDZ1_RAT] NMDA receptor subtype of glutamate-gated ion channels possesses high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. Plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors.[1]
About this Structure
3q41 is a 3 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
- Farina AN, Blain KY, Maruo T, Kwiatkowski W, Choe S, Nakagawa T. Separation of Domain Contacts Is Required for Heterotetrameric Assembly of Functional NMDA Receptors. J Neurosci. 2011 Mar 9;31(10):3565-79. PMID:21389213 doi:10.1523/JNEUROSCI.6041-10.2011
- ↑ Inanobe A, Furukawa H, Gouaux E. Mechanism of partial agonist action at the NR1 subunit of NMDA receptors. Neuron. 2005 Jul 7;47(1):71-84. PMID:15996549 doi:10.1016/j.neuron.2005.05.022
