Sandbox Reserved 1649: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 13: | Line 13: | ||
ATD allow to modulate NMDA receptor. Difference between différents NR2 is mainly regulated by ATD because diversity of ATD can modulate traffic in endoplasmic reticulum ans then affect the localisation of NMDAr. ATD of NR2A increase glutamate affinity, control channel’s opening with high probability and open duration, control glutamate deactivationtime course.<ref name="ATD function">DOI 10.1523/JNEUROSCI.1365-09.2009</ref> <ref name="ATD RE">DOI 10.1051/medsci/201026165</ref> | ATD allow to modulate NMDA receptor. Difference between différents NR2 is mainly regulated by ATD because diversity of ATD can modulate traffic in endoplasmic reticulum ans then affect the localisation of NMDAr. ATD of NR2A increase glutamate affinity, control channel’s opening with high probability and open duration, control glutamate deactivationtime course.<ref name="ATD function">DOI 10.1523/JNEUROSCI.1365-09.2009</ref> <ref name="ATD RE">DOI 10.1051/medsci/201026165</ref> | ||
LBD is constitued of two domains S1 (localised juste upstream M1 transmembranaire domain) and S2 and has affinity for L-glutamate (lien wiki https://fr.wikipedia.org/wiki/Acide_glutamique) or sometime glycine. Positive charge of Amino-group of the agonist bind to negativ charges residue of the pocket D731. In GlurR, negative charge amino acid is a E731 and is able to form salt bridge with agonist. In NR2A D731 is not able to do salt bridge with amino group because aspartate is one methylene lacking to do it. | LBD is constitued of two domains S1 (localised juste upstream M1 transmembranaire domain) and S2 and has affinity for L-glutamate (lien wiki https://fr.wikipedia.org/wiki/Acide_glutamique) or sometime glycine. Positive charge of Amino-group of the agonist bind to negativ charges residue of the pocket D731. In GlurR, negative charge amino acid is a E731 and is able to form salt bridge with agonist. In NR2A D731 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 E413 and Y761. 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 agonist is stabilised by water mediated hydrogen bonds to amino acid E413 and Y761. 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> | |||
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 | 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 | ||
