3q41

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[[Image:3q41.jpg|left|200px]]
 
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{{STRUCTURE_3q41| PDB=3q41 | SCENE= }}
{{STRUCTURE_3q41| PDB=3q41 | SCENE= }}
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===Crystal structure of the GluN1 N-terminal domain (NTD)===
===Crystal structure of the GluN1 N-terminal domain (NTD)===
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{{ABSTRACT_PUBMED_21389213}}
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==Function==
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[[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>
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{{ABSTRACT_PUBMED_21389213}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:21389213</ref><references group="xtra"/>
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<ref group="xtra">PMID:021389213</ref><references group="xtra"/><references/>
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Blain, K Y.]]
[[Category: Blain, K Y.]]
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[[Category: Maruo, T.]]
[[Category: Maruo, T.]]
[[Category: Nakagawa, T.]]
[[Category: Nakagawa, T.]]
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[[Category: Glun1]]
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[[Category: Glycosylation]]
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[[Category: Ion channel]]
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[[Category: Nmda]]
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[[Category: Ntd]]
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[[Category: Transport protein]]

Revision as of 08:09, 8 May 2013

Template:STRUCTURE 3q41

Contents

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
  1. 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

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