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. 2021 May 20;153(6):e202012742. doi: 10.1085/jgp.202012742

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© 2021 Szanto et al.

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Figure 1. — Structure of the pore region of K_v1.2. The S6 segments of two diagonally opposed subunits are shown as ribbon representations with front and rear subunits removed for clarity. The pore domain consists of the selectivity filter at the top, the water-filled cavity below, and the activation gate at the bottom. The latter is formed by the crossing of the S6 helices of each of the four subunits at the intracellular end of the pore (bundle crossing). Residues that are involved in the stabilization of the inactivated conformation of the selectivity filter region (Val443, Tyr445, and Asp447) are illustrated in stick format along with other residues important for the study (Trp434, Trp435, Thr449, and Ile470).