Structural modeling predicts that the GluN2B-C456Y mutation disrupts a disulfide bond between the ATD and LBD.
figureposted on 2020-04-30, 17:52 authored by Wangyong Shin, Kyungdeok Kim, Benjamin Serraz, Yi Sul Cho, Doyoun Kim, Muwon Kang, Eun-Jae Lee, Hyejin Lee, Yong Chul Bae, Pierre Paoletti, Eunjoon Kim
(A and B) Molecular modeling of the GluN2B-C456Y protein in complex with the GluN1 subunit of NMDARs. Note that the two cysteine residues in patch 1 of the LBD and patch 2 of the ATD in the WT GluN2B protein form a disulfide bond that strengthens the interaction between LBD and ATD, a bond that is disrupted by the GluN2B-C456Y mutation in patch 1 of the LBD. ATD, amino-terminal domain; LBD, ligand-binding domain; NMDAR, N-methyl-D-aspartate receptor; WT, wild type.
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