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. 2018 Nov 5;38(2):e99894. doi: 10.15252/embj.201899894

Figure 5. Structural mobility of an inter‐layer GluN1 protruding loop during rolling.

Figure 5

  1. Left, localization of interface 1 between GluN1 ABD and GluN2B NTD. This interface involves a GluN1‐specific loop that protrudes from GluN1 ABD upper lobe toward GluN2B NTD lower lobe. Right, initial and final frames of the fitting presented in Fig 4 at interface 1. The two pairs of residues targeted for cysteine mutations GluN1‐N492/GluN2B‐S188 and GluN1‐K495/GluN2B‐N192 are shown as spheres linked by a dotted line colored black and red, respectively.
  2. Evolution of Cα‐Cα distances of the two pairs of residues GluN1‐N492/GluN2B‐S188 and GluN1‐K495/GluN2B‐N192 during the fitting.
  3. MK‐801 inhibition kinetics. On‐rate constants (k on) of inhibition by 10 nM MK‐801 on wild‐type (WT) and mutant receptors. All values are normalized to that obtained for WT GluN1/GluN2B receptors. Values of Mean and n are given in Appendix Table S2. *P < 0.05, one‐way ANOVA on ranks followed by Bonferroni‐corrected Dunn's test. Error bars, SD.