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

. 2020 May 18;11:2478. doi: 10.1038/s41467-020-16288-4

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

© The Author(s) 2020

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/.

PMC Copyright notice

Fig. 5 — a Side views of one hSOAT1 subunit in cartoon representation. The transmembrane helices are colored in the same way as in Fig. 3c, d. The inhibitor CI-976 is shown in lemon sphere. b Close-up view of CI-976 binding sites. Residues that interact with CI-976 are shown as sticks. c Electron density of CI-976 and catalytic H460 were shown in blue meshes at the same contour level. Maps were further sharpened at −50 Å2 by Coot for visualization. d A 90° rotated view of c, density of H460 was omitted. e The thermostability enhancement effect of CI-976 on various hSOAT1 dimer mutants. The thermostability enhancement index was calculated by dividing dimer/monomer peak height ratio in the presence of CI-976 with the peak height ratio in the presence of DMSO alone (Data are shown as means± standard deviations, n = 3 biologically independent samples, ****p < 0.0001 for N421A; p = 0.0027 for H460A; p = 0.0100 for H460N respectively, two-tailed paired t-tests). f Close-up view of the M6-αD loop and αD with side chains shown in sticks. Residues that are important for SOAT1 enzyme activity reported in g were colored in green. g Enzymatic activities of various hSOAT1 mutants. (For D406A, n = 4. For W407A, n = 4. For W408A, n = 5. For N409A, n = 8. For S410C, n = 6. For S412A, n = 3. For S414C, n = 6. For Y416A, n = 4. For Y417A, n = 4. For R418A, n = 4. For W420A, n = 3. For N421A, n = 4. For V422A, n = 5 biologically independent samples.) Data are shown as means ± standard errors. A two-tailed unpaired t test was used to calculate the p values. For S410C, p = 0.9434. For S412A, p = 0.017. Other mutants had p values less than 0.0001. The expression levels of hSOAT1 mutants and endogenous vinculin are shown below. The original blots were provided as a Source Data file. h, i The top and side views of one hSOAT1 monomer in the surface representation. The surfaces are colored by electrostatic potential calculated by Pymol. j The cut-away view showing the binding pocket of the inhibitor CI-976 inside the reaction chamber. Source data are provided as a Source Data file.