2a5t

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(New page: 200px<br /><applet load="2a5t" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a5t, resolution 2.00&Aring;" /> '''Crystal Structure Of...)
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[[Image:2a5t.gif|left|200px]]<br /><applet load="2a5t" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2a5t, resolution 2.00&Aring;" />
 
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'''Crystal Structure Of The NR1/NR2A ligand-binding cores complex'''<br />
 
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==Overview==
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==Crystal Structure Of The NR1/NR2A ligand-binding cores complex==
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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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<StructureSection load='2a5t' size='340' side='right'caption='[[2a5t]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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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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</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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<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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<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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== 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/initialview03.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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==About this Structure==
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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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2A5T is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with GLY and GLU as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A5T OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16281028 16281028]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 2a5t" style="background-color:#fffaf0;"></div>
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[[Category: Rattus norvegicus]]
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[[Category: Furukawa, H.]]
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[[Category: Gouaux, E.]]
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[[Category: Mancusso, R.]]
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[[Category: Singh, S.K.]]
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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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:56:00 2007''
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==See Also==
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*[[Glutamate receptor 3D structures|Glutamate receptor 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Canis lupus familiaris]]
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[[Category: Large Structures]]
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[[Category: Rattus norvegicus]]
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[[Category: Furukawa H]]
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[[Category: Gouaux E]]
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[[Category: Mancusso R]]
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[[Category: Singh SK]]

Current revision

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

PDB ID 2a5t

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