Structural basis for substrate recognition mechanism of human SLC26A7

• Published in: Nature communications Vol. 16; no. 1; pp. 7600 - 10
• Main Authors: Li, Xiaorong, Yang, Xiaoxu, Lu, Xiaoli, Lin, Bingqian, Zhang, Yuanyuan, Huang, Bangdong, Zhou, Yutong, Huang, Jing, Wu, Kun, Zhou, Qiang, Chi, Ximin
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 15.08.2025; Nature Publishing Group; Nature Portfolio
• Subjects: 101/28; 631/45/535/1258; 631/45/612; 82/80; 82/83; 9/74; Bicarbonates; Binding Sites; Chloride; Chlorides; Chlorides - metabolism; Congenital diseases; Cryoelectron Microscopy; HEK293 Cells; Humanities and Social Sciences; Humans; Iodides; Iodides - chemistry; Iodides - metabolism; Ions; Kidney stones; Molecular dynamics; Molecular Dynamics Simulation; multidisciplinary; Mutation; Nitrates; Protein Binding; Protein transport; Proteins; Recognition; Science; Science (multidisciplinary); Substrate Specificity; Sulfate Transporters - chemistry; Sulfate Transporters - genetics; Sulfate Transporters - metabolism; Thyroid gland; Transmembrane proteins

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 S...