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' /> ==NR2A (2A5S)==

== NR2A (2A5S) ==

NR2A is a protein which forms an heterodimers channel with NR1 protein , the gathering of this two subnits formed [https://en.wikipedia.org/wiki/NMDA_receptor NMDA receptors] which is essential for Ca2+ influx in synapses thanks to glutamate and glycine binding 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 constitued of two domains S1 (localised juste upstream M1 transmembranaire domain) and S2 and has affinity for glutamate or sometime glycine. Positive charge of Amino-group of the agonist bind to negativ 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 D731 (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 stabilised by water mediated hydrogen bonds to amino acid Y761 (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 T114 et S112.

LBD is constitued of two domains S1 (localised juste upstream M1 transmembranaire domain) and S2 and has affinity for glutamate or sometime glycine. Positive charge of Amino-group of the agonist bind to negativ 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 D731 (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 stabilised by water mediated hydrogen bonds to amino acid Y761 (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 S112.

'''Transmembrane domain'''

Sandbox Reserved 1649: Difference between revisions

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@@ Line 1: / Line 1: @@
-<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)==
+<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 forms an heterodimers channel with NR1 protein , the gathering of this two subnits formed [https://en.wikipedia.org/wiki/NMDA_receptor NMDA receptors] which is essential for Ca2+ influx in synapses thanks to glutamate and glycine binding 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 14: / Line 15: @@
 '''Ligand binding domain (LBD)'''
-LBD is constitued of two domains S1 (localised juste upstream M1 transmembranaire domain) and S2 and has affinity for glutamate or sometime glycine. Positive charge of Amino-group of the agonist bind to negativ 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 D731 (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 stabilised by water mediated hydrogen bonds to amino acid Y761 (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 T114 et S112.
+LBD is constitued of two domains S1 (localised juste upstream M1 transmembranaire domain) and S2 and has affinity for glutamate or sometime glycine. Positive charge of Amino-group of the agonist bind to negativ 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 D731 (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 stabilised by water mediated hydrogen bonds to amino acid Y761 (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 S112.
 '''Transmembrane domain'''