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2a5t

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Revision as of 05:04, 16 November 2017

Crystal Structure Of The NR1/NR2A ligand-binding cores complex

Structural highlights

2a5t is a 2 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1pb7, 2a5s
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Excitatory neurotransmission mediated by NMDA (N-methyl-D-aspartate) receptors is fundamental to the physiology of the mammalian central nervous system. These receptors are heteromeric ion channels that for activation require binding of glycine and glutamate to the NR1 and NR2 subunits, respectively. NMDA receptor function is characterized by slow channel opening and deactivation, and the resulting influx of cations initiates signal transduction cascades that are crucial to higher functions including learning and memory. Here we report crystal structures of the ligand-binding core of NR2A with glutamate and that of the NR1-NR2A heterodimer with glutamate and glycine. The NR2A-glutamate complex defines the determinants of glutamate and NMDA recognition, and the NR1-NR2A heterodimer suggests a mechanism for ligand-induced ion channel opening. Analysis of the heterodimer interface, together with biochemical and electrophysiological experiments, confirms that the NR1-NR2A heterodimer is the functional unit in tetrameric NMDA receptors and that tyrosine 535 of NR1, located in the subunit interface, modulates the rate of ion channel deactivation.

Subunit arrangement and function in NMDA receptors.,Furukawa H, Singh SK, Mancusso R, Gouaux E Nature. 2005 Nov 10;438(7065):185-92. PMID:16281028^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ Furukawa H, Singh SK, Mancusso R, Gouaux E. Subunit arrangement and function in NMDA receptors. Nature. 2005 Nov 10;438(7065):185-92. PMID:16281028 doi:10.1038/nature04089

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a5t"

@@ Line 1: / Line 1: @@
 ==Crystal Structure Of The NR1/NR2A ligand-binding cores complex==
 <StructureSection load='2a5t' size='340' side='right' caption='[[2a5t]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pb7|1pb7]], [[2a5s|2a5s]]</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=2a5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a5t OCA], [http://pdbe.org/2a5t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a5t RCSB], [http://www.ebi.ac.uk/pdbsum/2a5t PDBsum]</span></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=2a5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a5t OCA], [http://pdbe.org/2a5t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a5t RCSB], [http://www.ebi.ac.uk/pdbsum/2a5t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a5t ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 2a5t" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Ionotropic Glutamate Receptors|Ionotropic Glutamate Receptors]]
 == References ==
 <references/>

2a5t

From Proteopedia

Revision as of 05:04, 16 November 2017

Crystal Structure Of The NR1/NR2A ligand-binding cores complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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