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. Author manuscript; available in PMC: 2019 Feb 15.
Published in final edited form as: Nature. 2018 Aug 15;560(7719):447–452. doi: 10.1038/s41586-018-0420-8

Extended Data Fig. 6. Inter-subunit interactions in Orco and Kv channels.

Extended Data Fig. 6

a, Top views of Orco (left) and Kv10.1 (Eag1)65 (right) highlighting the overall organization of these tetrameric cation channels. In this Kv channel, the pore and voltage-domains are not domain-swapped and so it more closely resembles the quaternary structure of Orco compared to other Kv channels. b, Top and c, side views showing inter-subunit interactions. Residues within 5 Å of a different subunit within the transmembrane region are shown as coloured spheres (16 residues in Orco, 58 residues in Kv10.1). In Orco, residues at subunit interfaces in the anchor domain are grey spheres (35 residues). The extracellular and intracellular domains of Kv10.1 are not shown.