2nr1

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[[Image:2nr1.png|left|200px]]
 
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{{STRUCTURE_2nr1| PDB=2nr1 | SCENE= }}
{{STRUCTURE_2nr1| PDB=2nr1 | SCENE= }}
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===TRANSMEMBRANE SEGMENT 2 OF NMDA RECEPTOR NR1, NMR, 10 STRUCTURES===
===TRANSMEMBRANE SEGMENT 2 OF NMDA RECEPTOR NR1, NMR, 10 STRUCTURES===
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{{ABSTRACT_PUBMED_10201407}}
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==Disease==
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[[http://www.uniprot.org/uniprot/NMDZ1_HUMAN NMDZ1_HUMAN]] Defects in GRIN1 are the cause of mental retardation autosomal dominant type 8 (MRD8) [MIM:[http://omim.org/entry/614254 614254]]. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period.<ref>PMID:21376300</ref>
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==Function==
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[[http://www.uniprot.org/uniprot/NMDZ1_HUMAN NMDZ1_HUMAN]] NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein 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 (By similarity).
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(as it appears on PubMed at http://www.pubmed.gov), where 10201407 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10201407}}
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==About this Structure==
==About this Structure==
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2NR1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NR1 OCA].
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[[2nr1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NR1 OCA].
==Reference==
==Reference==
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Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy., Opella SJ, Marassi FM, Gesell JJ, Valente AP, Kim Y, Oblatt-Montal M, Montal M, Nat Struct Biol. 1999 Apr;6(4):374-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10201407 10201407]
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<ref group="xtra">PMID:010201407</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
 
[[Category: Gesell, J J.]]
[[Category: Gesell, J J.]]
[[Category: Montal, M.]]
[[Category: Montal, M.]]
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[[Category: Postsynaptic membrane]]
[[Category: Postsynaptic membrane]]
[[Category: Receptor]]
[[Category: Receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:15:59 2008''
 

Revision as of 07:08, 25 March 2013

Template:STRUCTURE 2nr1

Contents

TRANSMEMBRANE SEGMENT 2 OF NMDA RECEPTOR NR1, NMR, 10 STRUCTURES

Template:ABSTRACT PUBMED 10201407

Disease

[NMDZ1_HUMAN] Defects in GRIN1 are the cause of mental retardation autosomal dominant type 8 (MRD8) [MIM:614254]. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period.[1]

Function

[NMDZ1_HUMAN] NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein 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 (By similarity).

About this Structure

2nr1 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

  • Opella SJ, Marassi FM, Gesell JJ, Valente AP, Kim Y, Oblatt-Montal M, Montal M. Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat Struct Biol. 1999 Apr;6(4):374-9. PMID:10201407 doi:10.1038/7610
  1. ↑ Hamdan FF, Gauthier J, Araki Y, Lin DT, Yoshizawa Y, Higashi K, Park AR, Spiegelman D, Dobrzeniecka S, Piton A, Tomitori H, Daoud H, Massicotte C, Henrion E, Diallo O, Shekarabi M, Marineau C, Shevell M, Maranda B, Mitchell G, Nadeau A, D'Anjou G, Vanasse M, Srour M, Lafreniere RG, Drapeau P, Lacaille JC, Kim E, Lee JR, Igarashi K, Huganir RL, Rouleau GA, Michaud JL. Excess of de novo deleterious mutations in genes associated with glutamatergic systems in nonsyndromic intellectual disability. Am J Hum Genet. 2011 Mar 11;88(3):306-16. doi: 10.1016/j.ajhg.2011.02.001. Epub, 2011 Mar 3. PMID:21376300 doi:10.1016/j.ajhg.2011.02.001

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