2a5t
From Proteopedia
(New page: 200px<br /><applet load="2a5t" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a5t, resolution 2.00Å" /> '''Crystal Structure Of...) |
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| - | [[Image:2a5t.gif|left|200px]]<br /><applet load="2a5t" size=" | + | [[Image:2a5t.gif|left|200px]]<br /><applet load="2a5t" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2a5t, resolution 2.00Å" /> | caption="2a5t, resolution 2.00Å" /> | ||
'''Crystal Structure Of The NR1/NR2A ligand-binding cores complex'''<br /> | '''Crystal Structure Of The NR1/NR2A ligand-binding cores complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Excitatory neurotransmission mediated by NMDA (N-methyl-D-aspartate) | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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 <scene name='pdbligand=GLY:'>GLY</scene> and <scene name='pdbligand=GLU:'>GLU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A5T OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gouaux, E.]] | [[Category: Gouaux, E.]] | ||
[[Category: Mancusso, R.]] | [[Category: Mancusso, R.]] | ||
| - | [[Category: Singh, S | + | [[Category: Singh, S K.]] |
[[Category: GLU]] | [[Category: GLU]] | ||
[[Category: GLY]] | [[Category: GLY]] | ||
[[Category: protein-ligand complex]] | [[Category: protein-ligand complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:23:51 2008'' |
Revision as of 14:23, 21 February 2008
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Crystal Structure Of The NR1/NR2A ligand-binding cores complex
Overview
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.
About this Structure
2A5T is a Protein complex structure of sequences from Rattus norvegicus with and as ligands. Full crystallographic information is available from OCA.
Reference
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
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