Difference between revisions of "Glutamate receptor ionotropic, NMDA 1"

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===Protein Function ===
 
===Protein Function ===
 
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. (From Uniprot)<br/>
 
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. (From Uniprot)<br/>
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[[File:549-function.png|center|600px]]
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[[File:549-function.png|center|500px]]
  
 
===Cys Function & Property===
 
===Cys Function & Property===

Revision as of 02:49, 10 August 2019

Basic Information
Short Name Glun1, GRIN1, NMDA1
UNP ID Q05586
Organism Homo sapiens
Cys Site Cys744, Cys798
Family/Domain Glutamate-gated ion channel family,
NR1/GRIN1 subfamily
Known Ligand Ligand list
Function Type Ion channel

Summary

Protein Function

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. (From Uniprot)

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Cys Function & Property

  • Hydrophobic property:
549-hydro.png
  • SASA：
Cys744: Unknown
Cys798: Unknown

Protein Sequence

MSTMRLLTLA LLFSCSVARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN
KRHGSWKIQL NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND
HFTPTPVSYT AGFYRIPVLG LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV
WFEMMRVYSW NHIILLVSDD HEGRAAQKRL ETLLEERESK AEKVLQFDPG
TKNVTALLME AKELEARVII LSASEDDAAT VYRAAAMLNM TGSGYVWLVG
EREISGNALR YAPDGILGLQ LINGKNESAH ISDAVGVVAQ AVHELLEKEN
ITDPPRGCVG NTNIWKTGPL FKRVLMSSKY ADGVTGRVEF NEDGDRKFAN
YSIMNLQNRK LVQVGIYNGT HVIPNDRKII WPGGETEKPR GYQMSTRLKI
VTIHQEPFVY VKPTLSDGTC KEEFTVNGDP VKKVICTGPN DTSPGSPRHT
VPQCCYGFCI DLLIKLARTM NFTYEVHLVA DGKFGTQERV NNSNKKEWNG
MMGELLSGQA DMIVAPLTIN NERAQYIEFS KPFKYQGLTI LVKKEIPRST
LDSFMQPFQS TLWLLVGLSV HVVAVMLYLL DRFSPFGRFK VNSEEEEEDA
LTLSSAMWFS WGVLLNSGIG EGAPRSFSAR ILGMVWAGFA MIIVASYTAN
LAAFLVLDRP EERITGINDP RLRNPSDKFI YATVKQSSVD IYFRRQVELS
TMYRHMEKHN YESAAEAIQA VRDNKLHAFI WDSAVLEFEA SQKCDLVTTG
ELFFRSGFGI GMRKDSPWKQ NVSLSILKSH ENGFMEDLDK TWVRYQECDS
RSNAPATLTF ENMAGVFMLV AGGIVAGIFL IFIEIAYKRH KDARRKQMQL
AFAAVNVWRK NLQDRKSGRA EPDPKKKATF RAITSTLASS FKRRRSSKDT
STGGGRGALQ NQKDTVLPRR AIEREEGQLQ LCSRHRES

Structural Information

  • Known structure with covalent ligand:
Unknown
  • Protein structure:
Unknown

Related Pathway

Experimental Evidence

Cys-directed Mutation

Reference

  1. Kim W K, Choi Y B, Rayudu P V, et al. Attenuation of NMDA receptor activity and neurotoxicity by nitroxyl anion, NO−[J]. Neuron, 1999, 24(2): 461-469. 10571239
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