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. 2019 Oct 1;9:14128. doi: 10.1038/s41598-019-49912-5

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© The Author(s) 2019

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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The PIRT polybasic C-terminal helix binds PIP₂. (a) Overlay of eight ¹⁵N-TROSY HSQC hPIRT NMR spectra colored as a function of increasing PIP₂ concentration. The left inset shows changes in H120 resonance position as the lipid is titrated. (b) Representative chemical shift perturbation (Δδ) titration plots for hPIRT K131 and H120 which are fit to a single binding site model as described in the methods. (c) hPIRT residues that specifically bind PIP₂ are highlighted red on the topology plot.