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==CRYSTAL STRUCTURE OF AMINO TERMINAL DOMAINS OF THE NMDA RECEPTOR SUBUNIT GLUN1 AND GLUN2B IN COMPLEX WITH MK-22==
==CRYSTAL STRUCTURE OF AMINO TERMINAL DOMAINS OF THE NMDA RECEPTOR SUBUNIT GLUN1 AND GLUN2B IN COMPLEX WITH MK-22==
<StructureSection load='5ewl' size='340' side='right' caption='[[5ewl]], [[Resolution|resolution]] 2.98&Aring;' scene=''>
<StructureSection load='5ewl' size='340' side='right'caption='[[5ewl]], [[Resolution|resolution]] 2.98&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ewl]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EWL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EWL FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ewl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EWL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5SL:~{N}-[(1~{S},3~{S})-3-[3-[(4-METHYLPHENYL)METHYL]-1,2,4-OXADIAZOL-5-YL]CYCLOPENTYL]-1~{H}-PYRAZOLO[3,4-D]PYRIMIDIN-4-AMINE'>5SL</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.98&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ewj|5ewj]], [[5ewm|5ewm]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5SL:~{N}-[(1~{S},3~{S})-3-[3-[(4-METHYLPHENYL)METHYL]-1,2,4-OXADIAZOL-5-YL]CYCLOPENTYL]-1~{H}-PYRAZOLO[3,4-D]PYRIMIDIN-4-AMINE'>5SL</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ewl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ewl OCA], [http://pdbe.org/5ewl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ewl RCSB], [http://www.ebi.ac.uk/pdbsum/5ewl PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ewl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ewl OCA], [https://pdbe.org/5ewl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ewl RCSB], [https://www.ebi.ac.uk/pdbsum/5ewl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ewl ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/NMDE2_HUMAN NMDE2_HUMAN]] Autosomal dominant non-syndromic intellectual disability;West syndrome. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  A chromosomal aberrations involving GRIN2B has been found in patients with mental retardation. Translocations t(9;12)(p23;p13.1) and t(10;12)(q21.1;p13.1) with a common breakpoint in 12p13.1.
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/NMDE2_HUMAN NMDE2_HUMAN]] NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death (By similarity).  
[https://www.uniprot.org/uniprot/NMDZ1_XENLA NMDZ1_XENLA] Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:16214956, PubMed:19524674, PubMed:21677647, PubMed:25008524, PubMed:26912815, PubMed:27135925, Ref.11, PubMed:28232581). Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable).<ref>PMID:16214956</ref> <ref>PMID:19524674</ref> <ref>PMID:21677647</ref> <ref>PMID:25008524</ref> <ref>PMID:26912815</ref> <ref>PMID:27135925</ref> <ref>PMID:28232581</ref> [PDB:5IOV]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5ewl" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5ewl" style="background-color:#fffaf0;"></div>
==See Also==
*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pandit, J]]
[[Category: Homo sapiens]]
[[Category: Allosteric inhibition]]
[[Category: Large Structures]]
[[Category: Glun2b subunit]]
[[Category: Xenopus laevis]]
[[Category: Nmda receptor]]
[[Category: Pandit J]]
[[Category: Transport protein]]
Retrieved from "https://proteopedia.org/5ewl"