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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 6. Overall conformational changes of the TMD.

Figure 6

Str-, gly- and gly/ivm-bound states are in blue, yellow and red, respectively. Comparison between str- and gly-GlyR (a), str- and gly/ivm-GlyR (b), gly- and gly/ivm-GlyR (c), viewed from the extracellular side. Side chains of −2′Pro and 9′Leu are shown in sticks to denote the change of pore sizes. In going from the str- to the gly-bound form, the TMD of each individual subunit undergoes a counter-clockwise outward rotation, enlarging the pore size by ‘pulling’ the side chains of 9′Leu and −2′Pro away from the channel axis. Binding of ivermectin to the gly-GlyR causes a clockwise inward rotation of the TMD. As a result, while the extracellular half of the pore undergoes little change, the intracellular entrance shrinks.