Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2023 Sep 27;622(7982):410–417. doi: 10.1038/s41586-023-06582-8

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© This is a U.S. Government work and not under copyright protection in the US; foreign copyright protection may apply 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Extended Data Fig. 6 — a) Superimposition of Kv2.1 (gray) with each of the four protomers of the L403A mutant aligned using the VSDs. b) Cryo-EM map of a single subunit of Kv2.1 (gray) with the map for protomer D in the L403A mutant (red). c) Conformational changes at the interface between S5 and S6 helices between Kv2.1 (gray) and protomer D of the L403A mutant (red). d) Conformational changes in the S6 helix between Kv2.1 (gray) and protomer D of the L403A mutant (red). Cryo-EM maps for S6 helices from protomer D in the L403A mutant (red) and Kv2.1 (gray) are shown to the right. e,f) A symmetrical L403A tetramer generated by aligning four D protomers to Kv2.1 based on selectivity filter. Dash lines indicate clashes between neighboring I405 side chains (e), between the sidechain of L329 and backbone of G312 (f) and between the sidechain of F333 and that of L313 (f). g,h) A symmetrical L403A tetramer modeled by aligning four D protomers to Kv2.1 based on the VSDs. Dash lines show clashes between neighboring I405 side chains (g) and distances between backbone carbonyls within the selectivity filter that are shorter when compared to those of Kv2.1 and other K⁺ channels whose filters are thought to be conducting (h).