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2a5t

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[[Image:2a5t.gif|left|200px]]
 
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{{Structure
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==Crystal Structure Of The NR1/NR2A ligand-binding cores complex==
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|PDB= 2a5t |SIZE=350|CAPTION= <scene name='initialview01'>2a5t</scene>, resolution 2.00&Aring;
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<StructureSection load='2a5t' size='340' side='right'caption='[[2a5t]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GLY:GLYCINE'>GLY</scene> and <scene name='pdbligand=GLU:GLUTAMIC ACID'>GLU</scene>
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<table><tr><td colspan='2'>[[2a5t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A5T FirstGlance]. <br>
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|ACTIVITY=
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</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&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a5t OCA], [https://pdbe.org/2a5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a5t RCSB], [https://www.ebi.ac.uk/pdbsum/2a5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a5t ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a5/2a5t_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2a5t ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Crystal Structure Of The NR1/NR2A ligand-binding cores complex'''
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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<ref>PMID:16281028</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2a5t" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2A5T is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A5T OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Canis lupus familiaris]]
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Subunit arrangement and function in NMDA receptors., Furukawa H, Singh SK, Mancusso R, Gouaux E, Nature. 2005 Nov 10;438(7065):185-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16281028 16281028]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Furukawa, H.]]
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[[Category: Furukawa H]]
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[[Category: Gouaux, E.]]
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[[Category: Gouaux E]]
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[[Category: Mancusso, R.]]
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[[Category: Mancusso R]]
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[[Category: Singh, S K.]]
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[[Category: Singh SK]]
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[[Category: GLU]]
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[[Category: GLY]]
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[[Category: protein-ligand complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:45:43 2008''
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Current revision

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

PDB ID 2a5t

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