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. Author manuscript; available in PMC: 2016 Apr 8.
Published in final edited form as: Nature. 2015 Sep 7;526(7572):224–229. doi: 10.1038/nature14853

Figure 4. Conformational changes within an individual subunit.

Figure 4

Str-, gly- and ivm/gly-bound states are in blue, yellow and red, respectively. a–c, Superimposition of the three GlyR structures using the ECD (residues 1-235), showing the motion of TMD. Relative rotation angles of the pore-lining M2 are indicated. Conformational changes in the ECD-TMD interface upon transition from the gly- (or gly/ivm-) to the str-bound states are shown in panels d and e, viewed parallel to the membrane and from the extracellular side, respectively. The displacement of the β8-β9 loop leads to a rotation of pre-M1/M1, pushing the lower half of M2 toward the pore axis; meanwhile, this displacement repositions the Cys loop through β10, which results in the coupling of the M2-M3 loop with the β1-β2 loop through the interaction between Pro291 and Thr70. Consequently, the upper half of M2 rotates outward.