Sandbox Reserved 1649: Difference between revisions
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LBD is constitued of two domains S1 (localised juste upstraem M1 transmembranaire domain) and S2 and has affinity for L-glutamate 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 upstraem M1 transmembranaire domain) and S2 and has affinity for L-glutamate 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. | 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+ | 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+ | ||
