Sandbox Reserved 1649: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
== 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), cytoplasmic re-entrant pore loop (M2), and an intracellular C-terminal domain (CTD). [[Image: | 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), cytoplasmic re-entrant pore loop (M2), and an intracellular C-terminal domain (CTD). [[Image:StructureNR2A3.jpg#filehistory| thumb |left|250px| upright=10|'''NR2A submit structure''']] | ||
'''Amino-terminal domain (ATD)''' | '''Amino-terminal domain (ATD)''' | ||
| Line 19: | Line 19: | ||
'''Transmembrane domain''' | '''Transmembrane domain''' | ||
The transmembrane domain is organized into 4 parts (from M1 to M4). | The transmembrane domain is organized into 4 parts (from M1 to M4). M1 connects the N terminal domain to M2. M2 forms a reentrant loop contributing to the pore. The S1 segment of the N terminal domain intertwines with the S2 segment of the GlnBP-type domain in the extracellular loop M3 - M4 to form the glutamate binding pocket. On the other hand, desensitization of NMDA receptors is affected by residues near or inside the binding pocket as well as by residues in M2 that line the pore and the M3 loop - M4 is not responsible for the specificity of the NR2 subunit of glycine independent desensitization.<ref name="transmembrane domain">DOI 10.1016/S0896-6273(00)80459-6</ref> | ||
M2 loop is a channel-lining loop and located in transmembranaire domain. Two asparagines are located on N site of the domain and block Mg2+ and are permeable of Ca2+ <ref name="M2loop">DOI 10.3390/ijms21041538</ref> | M2 loop is a channel-lining loop and located in transmembranaire domain. Two asparagines are located on N site of the domain and block Mg2+ and are permeable of Ca2+ <ref name="M2loop">DOI 10.3390/ijms21041538</ref> | ||
