Sandbox Reserved 1649: Difference between revisions

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== Structure and Function ==
== Structure and Function ==


NR2A (GluN2A) is composed of Amino-terminal domain (ATD), segments S1 and S2 which formed ligand binding domain of glutamate, three transmembrane helices (M1, M3,and M4), a cytoplasmic re-entrant pore loop (M2), and an intracellular C-terminal domain (CTD). [[Image:StructureNR2A4.jpg#filehistory| thumb |left|360px| upright=10|'''NR2A submit structure''']]
NR2A (GluN2A) is composed of an amino-terminal domain (ATD), segments S1 and S2 which formed ligand binding domain of glutamate, three transmembrane helices (M1, M3,and M4), a cytoplasmic re-entrant pore loop (M2), and an intracellular C-terminal domain (CTD). [[Image:StructureNR2A4.jpg#filehistory| thumb |left|360px| upright=10|'''NR2A submit structure''']]


'''Amino-terminal domain (ATD)'''  
'''Amino-terminal domain (ATD)'''  


The ATD is constituted by first 383 amino acids of NR2A. ATD is an alpha and beta protein class. Structure is bilobed and form clam-shell like structure which consists in two lobes linked by a flexible hinge region defining a central groove. <ref name="ATD clamshell">DOI 10.1038/nsmb.2522</ref> Zn2+ may insert between 2 lobes and induces closure of channel by changing conformation of ATD. Zn increases affinity of glutamate on the LBD which reminds the desensitization of [https://en.wikipedia.org/wiki/AMPA_receptor AMPA] and [https://en.wikipedia.org/wiki/Kainate_receptor Kainate receptor].  <ref name="Zn">DOI 10.1016/s0896-6273(00)00163-x</ref> <ref name="ATD RE">DOI 10.1051/medsci/201026165</ref>
The ATD is constituted by the first 383 amino acids of NR2A. ATD is an alpha and beta protein class. Its structure is bilobed and forms a clam-shell like structure which consists in two lobes linked by a flexible hinge region defining a central groove. <ref name="ATD clamshell">DOI 10.1038/nsmb.2522</ref> Zn2+ may insert between 2 lobes and induces closure of channel by changing conformation of ATD. Zn increases affinity of glutamate on the LBD which reminds the desensitization of [https://en.wikipedia.org/wiki/AMPA_receptor AMPA] and [https://en.wikipedia.org/wiki/Kainate_receptor Kainate receptor].  <ref name="Zn">DOI 10.1016/s0896-6273(00)00163-x</ref> <ref name="ATD RE">DOI 10.1051/medsci/201026165</ref>
ATD allows to modulate NMDA receptor. Difference between different NR2 is mainly regulated by ATD, because diversity of ATD can modulate traffic in endoplasmic reticulum and then affect the localization of NMDAr. ATD of NR2A increases glutamate affinity, control channel’s opening with high probability and open duration, control glutamate deactivation time course.<ref name="ATD function">DOI 10.1523/JNEUROSCI.1365-09.2009</ref>
ATD allows to modulate NMDA receptor. The difference between various NR2 is mainly regulated by ATD. Indeed, the diversity of ATD can modulate traffic in endoplasmic reticulum and then affect the localization of NMDAr. ATD of NR2A increases glutamate affinity, controls channel’s opening with high probability and open duration, control glutamate deactivation time course.<ref name="ATD function">DOI 10.1523/JNEUROSCI.1365-09.2009</ref>


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