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==Crystal structure of GluN1/GluN2A NMDA receptor agonist binding domains with glycine and antagonist, phenyl-ACEPC== | |||
<StructureSection load='5dex' size='340' side='right' caption='[[5dex]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5dex]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DEX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DEX FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5E0:5-[(2R)-2-AMINO-2-CARBOXYETHYL]-1-PHENYL-1H-PYRAZOLE-3-CARBOXYLIC+ACID'>5E0</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene></td></tr> | |||
[[Category: | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ddn|5ddn]], [[5ddx|5ddx]], [[5de4|5de4]]</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=5dex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dex OCA], [http://pdbe.org/5dex PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dex RCSB], [http://www.ebi.ac.uk/pdbsum/5dex PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dex ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[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. | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Conti, P]] | |||
[[Category: Hansen, K B]] | |||
[[Category: Mou, T C]] | |||
[[Category: Pinto, A]] | [[Category: Pinto, A]] | ||
[[Category: Sprang, S R]] | |||
[[Category: Tamborini, L]] | [[Category: Tamborini, L]] | ||
[[Category: | [[Category: Receptor]] | ||
[[Category: | [[Category: Transport protein]] | ||
Revision as of 18:28, 14 September 2016
Crystal structure of GluN1/GluN2A NMDA receptor agonist binding domains with glycine and antagonist, phenyl-ACEPCCrystal structure of GluN1/GluN2A NMDA receptor agonist binding domains with glycine and antagonist, phenyl-ACEPC
Structural highlights
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. References
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