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Structural basis for substrate recognition mechanism of human SLC26A7

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  • Xiaorong Li

    (Zhejiang University
    Westlake University, Westlake Laboratory of Life Sciences and Biomedicine
    Westlake Institute for Advanced Study)

  • Xiaoxu Yang

    (Westlake University, Westlake Laboratory of Life Sciences and Biomedicine
    Westlake Institute for Advanced Study)

  • Xiaoli Lu

    (Westlake University, Westlake Laboratory of Life Sciences and Biomedicine
    Westlake Institute for Advanced Study)

  • Bingqian Lin

    (Westlake University, Westlake Laboratory of Life Sciences and Biomedicine
    Westlake Institute for Advanced Study)

  • Yuanyuan Zhang

    (Zhejiang University
    Westlake University, Westlake Laboratory of Life Sciences and Biomedicine
    Westlake Institute for Advanced Study)

  • Bangdong Huang

    (Westlake University, Westlake Laboratory of Life Sciences and Biomedicine
    Westlake Institute for Advanced Study)

  • Yutong Zhou

    (Westlake University, Westlake Laboratory of Life Sciences and Biomedicine
    Westlake Institute for Advanced Study)

  • Jing Huang

    (Westlake University, Westlake Laboratory of Life Sciences and Biomedicine
    Westlake Institute for Advanced Study)

  • Kun Wu

    (Westlake University, Westlake Laboratory of Life Sciences and Biomedicine
    Westlake Institute for Advanced Study)

  • Qiang Zhou

    (Westlake University, Westlake Laboratory of Life Sciences and Biomedicine
    Westlake Institute for Advanced Study)

  • Ximin Chi

    (Xiamen University)

Abstract

Solute carrier family 26 (SLC26) mainly mediates transmembrane transport of various anion ions, including chloride and other halide ions, bicarbonate, oxalate, and sulfate. Many severe hereditary human diseases are correlated with SLC26 protein mutations. Here we report cryo-EM structures of human SLC26A7 in apo and iodide binding states. We identify non-canonical binding site for halide ions in SLC26A7. Molecular dynamics simulation and electrophysiological assay confirm the functional importance of key residues involved in iodide and chloride coordination. Together, our discovery marks a step towards an in-depth understanding of SLC26 family protein transport mechanisms.

Suggested Citation

  • Xiaorong Li & Xiaoxu Yang & Xiaoli Lu & Bingqian Lin & Yuanyuan Zhang & Bangdong Huang & Yutong Zhou & Jing Huang & Kun Wu & Qiang Zhou & Ximin Chi, 2025. "Structural basis for substrate recognition mechanism of human SLC26A7," Nature Communications, Nature, vol. 16(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-62792-w
    DOI: 10.1038/s41467-025-62792-w
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