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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

Extended Data Figure 8. Superimposition of TMD between str- and gly-GlyR (a), str- and gly/ivm-GlyR (b), gly- and gly/ivm-GlyR (c) using main chain atoms of residues Met236-Lys362.

Extended Data Figure 8

The M2-M3 loop, residues Ser289-Ala298, is excluded from the comparison. The r.m.s.d. are 0.9, 0.9 and 0.7 A, respectively, suggesting that the movement of the TMD is rigid-body-like. Most differences are located in the termini of transmembrane helices, which are either close to the M2-M3 loop, or close to the intracellular gate −2′Pro.