Sandbox Reserved 1649: Difference between revisions

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<scene name='86/868182/G731/1'>Text To Be Displayed</scene><Structure load='2A5S' size='350' frame='true' align='right' caption='Crystal Structure Of The NR2A Ligand Binding Core In Complex With Glutamate' scene='Insert optional scene name here' />

== NR2A (2A5S) ==

NR2A is a protein which is a part of [https://en.wikipedia.org/wiki/NMDA_receptor NMDA receptors], heterodimer channels composed of four subunits. Indeed, NMDA receptors are made of the association between two NR2 and two NR1 proteins. NMDA receptors play a key role in mammalian central nervous system, as they act in Ca2+ influx in synapses in response to glutamate and glycine binding. Their role is essential for learning and memory. Variety of NR2 allows modulation of NMDAr. In the other hand, [https://www.youtube.com/watch?fbclid=IwAR163EHEh3RM8BXt-_4aiecrCgkF83HoyOefyU63d_CQwoqN5RHShYfLDnM&v=4-DuvwoH2zQ&feature=youtu.be NMDA receptor is related to AMPA receptor in the same synapse.]

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'''Ligand binding domain (LBD)'''

LBD is constituted of two domains S1 (located juste upstream M1 transmembrane domain) and S2 and has affinity for glutamate or sometime glycine. Positive charge of amino-group of the agonist bind to negative charges residue of the pocket D731. In [https://proteopedia.org/wiki/index.php/Glutamate_receptor_%28GluA2%29 GlurR], negative charge amino acid is a E731 and is able to form salt bridge with agonist. In NR2A <scene name='~~D731~~'>D731</scene> (which corresponds to D213) is not able to do salt bridge with amino group because aspartate is one methylene lacking to do it. Amino group of agonist is stabilized by water mediated hydrogen bonds to amino acid <scene name='Y761'>Y761</scene> (which corresponds to Y243) and E413 (which correspond to E14). The high affinity for glutamate agonist may be because of van der Walls contact between γ-carboxylate group of glutamate and Y730 of S2 domain which is conserved in NR2 protein.<ref name="LBD">DOI 10.1038/nature04089</ref> Amino-group of glutamate also interacts with <scene name='T114'>T114</scene> et <scene name='S112'>S112</scene>.

LBD is constituted of two domains S1 (located juste upstream M1 transmembrane domain) and S2 and has affinity for glutamate or sometime glycine. Positive charge of amino-group of the agonist bind to negative charges residue of the pocket D731. In [https://proteopedia.org/wiki/index.php/Glutamate_receptor_%28GluA2%29 GlurR], negative charge amino acid is a E731 and is able to form salt bridge with agonist. In NR2A <scene name='86/868182/G731/1'>D731</scene> (which corresponds to D213) is not able to do salt bridge with amino group because aspartate is one methylene lacking to do it. Amino group of agonist is stabilized by water mediated hydrogen bonds to amino acid <scene name='Y761'>Y761</scene> (which corresponds to Y243) and E413 (which correspond to E14). The high affinity for glutamate agonist may be because of van der Walls contact between γ-carboxylate group of glutamate and Y730 of S2 domain which is conserved in NR2 protein.<ref name="LBD">DOI 10.1038/nature04089</ref> Amino-group of glutamate also interacts with <scene name='T114'>T114</scene> et <scene name='S112'>S112</scene>.

'''Transmembrane domain'''

Sandbox Reserved 1649: Difference between revisions

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-<Structure load='2A5S' size='350' frame='true' align='right' caption='Crystal Structure Of The NR2A Ligand Binding Core In Complex With Glutamate' scene='Insert optional scene name here' />
+<scene name='86/868182/G731/1'>Text To Be Displayed</scene><Structure load='2A5S' size='350' frame='true' align='right' caption='Crystal Structure Of The NR2A Ligand Binding Core In Complex With Glutamate' scene='Insert optional scene name here' />
 == NR2A (2A5S) ==
 NR2A is a protein which is a part of [https://en.wikipedia.org/wiki/NMDA_receptor NMDA receptors],  heterodimer channels composed of four subunits. Indeed, NMDA receptors are made of the association between two NR2 and two NR1 proteins. NMDA receptors play a key role in mammalian central nervous system, as they act in Ca2+ influx in synapses in response to glutamate and glycine binding. Their role is essential for learning and memory. Variety of NR2 allows modulation of NMDAr. In the other hand, [https://www.youtube.com/watch?fbclid=IwAR163EHEh3RM8BXt-_4aiecrCgkF83HoyOefyU63d_CQwoqN5RHShYfLDnM&v=4-DuvwoH2zQ&feature=youtu.be NMDA receptor is related to AMPA receptor in the same synapse.]
@@ Line 15: / Line 15: @@
 '''Ligand binding domain (LBD)'''
-LBD is constituted of two domains S1 (located juste upstream M1 transmembrane domain) and S2 and has affinity for glutamate or sometime glycine. Positive charge of amino-group of the agonist bind to negative charges residue of the pocket D731. In [https://proteopedia.org/wiki/index.php/Glutamate_receptor_%28GluA2%29 GlurR], negative charge amino acid is a E731 and is able to form salt bridge with agonist. In NR2A <scene name='D731'>D731</scene> (which corresponds to D213) is not able to do salt bridge with amino group because aspartate is one methylene lacking to do it. Amino group of agonist is stabilized by water mediated hydrogen bonds to amino acid <scene name='Y761'>Y761</scene> (which corresponds to Y243) and E413 (which correspond to E14). The high affinity for glutamate agonist may be because of van der Walls contact between γ-carboxylate group of glutamate and Y730 of S2 domain which is conserved in NR2 protein.<ref name="LBD">DOI 10.1038/nature04089</ref> Amino-group of glutamate also interacts with <scene name='T114'>T114</scene> et <scene name='S112'>S112</scene>.
+LBD is constituted of two domains S1 (located juste upstream M1 transmembrane domain) and S2 and has affinity for glutamate or sometime glycine. Positive charge of amino-group of the agonist bind to negative charges residue of the pocket D731. In [https://proteopedia.org/wiki/index.php/Glutamate_receptor_%28GluA2%29 GlurR], negative charge amino acid is a E731 and is able to form salt bridge with agonist. In NR2A <scene name='86/868182/G731/1'>D731</scene> (which corresponds to D213) is not able to do salt bridge with amino group because aspartate is one methylene lacking to do it. Amino group of agonist is stabilized by water mediated hydrogen bonds to amino acid <scene name='Y761'>Y761</scene> (which corresponds to Y243) and E413 (which correspond to E14). The high affinity for glutamate agonist may be because of van der Walls contact between γ-carboxylate group of glutamate and Y730 of S2 domain which is conserved in NR2 protein.<ref name="LBD">DOI 10.1038/nature04089</ref> Amino-group of glutamate also interacts with <scene name='T114'>T114</scene> et <scene name='S112'>S112</scene>.
 '''Transmembrane domain'''