Structural Basis for Inhibition of Human Anion Transporter SLC26A6/PAT-1

High-resolution cryo-EM structures of the human PAT-1 (SLC26A6) homodimer bound to DIDS and PAT1inh-B01 reveal distinct inhibition mechanisms and domain interactions.

• Why it matters: PAT-1 dysfunction is linked to nephrolithiasis and hyperoxaluria, and modulating this transporter is a potential therapeutic strategy for cystic fibrosis.
• What they did: The authors solved cryo-electron microscopy structures of human PAT-1 in complex with the two small-molecule inhibitors DIDS and PAT1inh-B01, comparing how each inhibitor engages the protein.
• The result: The inhibitor-bound structures clarify how transmembrane, STAS, and N-terminal domains interact, providing mechanistic insight into PAT-1 molecular function and inhibition.

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