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. 2018 Jun 5;4:27. doi: 10.1038/s41421-018-0026-1

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© The Author(s) 2018

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a Location of mambalgin-1 in cASIC1a^ΔNC-mambalgin-1 complex. A single subunit of cASIC1a channel is shown in surface representation with each domain in a different color. Mambalgin-1 is shown in ribbon representation. Insert, the location of mambalgin-1 (cyan) overlapping with PcTx1 (magenta). The PcTx1 position was taken from the structure of PcTx1-bound cASIC1a (PDB 4FZ1). b Cartoon representation of a single subunit derived from the cASIC1a^ΔNC-mambalgin-1 complex. c, d Close-up views of the interactions of the Finger I region (c) and Finger II region (d) of mambalgin-1 with the thumb domain of cASIC1a^ΔNC. The Cα atoms of several key residues in the finger regions are shown as spheres. Basic residues of mambalgin-1 fingers are colored in blue, and the hydrophobic residues in white. e Bar graph representing the effect of different mambalgin-1 point mutants (500 nM) on wild-type cASIC1a. Data are means±S.E. (error bars) (*P < 0.05; **P < 0.01; ***P < 0.001; different from WT; t-test; n = 4–13)