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. 2024 Aug 27;43(20):4699–4719. doi: 10.1038/s44318-024-00211-4

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© The Author(s) 2024

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/. Creative Commons Public Domain Dedication waiver http://creativecommons.org/publicdomain/zero/1.0/ applies to the data associated with this article, unless otherwise stated in a credit line to the data, but does not extend to the graphical or creative elements of illustrations, charts, or figures. This waiver removes legal barriers to the re-use and mining of research data. According to standard scholarly practice, it is recommended to provide appropriate citation and attribution whenever technically possible.

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(A) Alphafold-Multimer Model of the STIC2 dimer. STIC2 is shown in two orientations in cartoon representation with rainbow coloring from blue to red. (B) Interaction of Alb4 Motif III with STIC2. Shown is the STIC2 electrostatic surface (Connolly surface colored with APBS potential from red to blue (−4 to +4 kJ/mol/e)) together with a cartoon representation of Alb4C in green. Residues of Alb4 within 4 Å of STIC2 are shown as sticks and labeled. (C) Interacting residues investigated in the study. Shown is STIC2 as gray cartoon model (monomer A, light gray, monomer B darker gray), Alb4C as green cartoon. Interacting residues characterized experimentally are shown as yellow sticks and labeled. (D–F) Pull-down experiments using purified GST-STIC2 and Alb4C variants are shown in (D) or the indicated GST-STIC2 point mutation variants and Alb4C (E) or Alb3C (F). GST-eGFP was used as a control. Assays were conducted using glutathione sepharose beads. Load samples are shown by Coomassie stained SDS-Gels. Eluates were analyzed by SDS-PAGE and subsequent immunoblotting using the indicated antibodies. Coelution was quantified using ImageJ. Means and SDs were calculated from three independent experiments. Source data are available online for this figure.