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4nf8

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'''Unreleased structure'''
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{{STRUCTURE_4nf8| PDB=4nf8 | SCENE= }}
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===Crystal structure of GluN1/GluN2A ligand-binding domain in complex with glycine and glutamate in PEG2000MME===
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{{ABSTRACT_PUBMED_24462099}}
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The entry 4nf8 is ON HOLD until Paper Publication
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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> [[http://www.uniprot.org/uniprot/NMDE1_RAT NMDE1_RAT]] NMDA receptor subtype of glutamate-gated ion channels possesses high calcium permeability and voltage-dependent sensitivity to magnesium. Activation requires binding of agonist to both types of subunits.
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Authors: Jespersen, A., Tajima, N., Furukawa, H.
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==About this Structure==
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[[4nf8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NF8 OCA].
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Description: Crystal structure of GluN1/GluN2A ligand-binding domain in complex with glycine and glutamate in PEG2000MME
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==Reference==
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<ref group="xtra">PMID:024462099</ref><references group="xtra"/><references/>
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[[Category: Furukawa, H.]]
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[[Category: Jespersen, A.]]
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[[Category: Tajima, N.]]
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[[Category: Glycine and glutamate]]
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[[Category: Receptor]]
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[[Category: Transport protein]]

Revision as of 13:36, 12 March 2014

Template:STRUCTURE 4nf8

Contents

Crystal structure of GluN1/GluN2A ligand-binding domain in complex with glycine and glutamate in PEG2000MME

Template:ABSTRACT PUBMED 24462099

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] [NMDE1_RAT] NMDA receptor subtype of glutamate-gated ion channels possesses high calcium permeability and voltage-dependent sensitivity to magnesium. Activation requires binding of agonist to both types of subunits.

About this Structure

4nf8 is a 2 chain structure. Full crystallographic information is available from OCA.

Reference

  • Jespersen A, Tajima N, Fernandez-Cuervo G, Garnier-Amblard EC, Furukawa H. Structural insights into competitive antagonism in NMDA receptors. Neuron. 2014 Jan 22;81(2):366-78. doi: 10.1016/j.neuron.2013.11.033. PMID:24462099 doi:http://dx.doi.org/10.1016/j.neuron.2013.11.033
  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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