Structural mechanism of substrate binding and inhibition of human taurine transporter - PubMed
5 hours ago
- #Structural biology
- #Taurine transporter
- #Therapeutic target
- Taurine is a sulfur-containing amino acid with crucial roles in the body, transported by the taurine transporter (TauT).
- Dysregulation or mutations in TauT are linked to neurological disorders, cardiomyopathy, retinal degeneration, and cancer.
- The study presents structures of human TauT (hTauT) in substrate-free, taurine-bound, β-alanine-bound, and P4S-bound states.
- Taurine, β-alanine, and the inhibitor P4S all bind at the central substrate-binding site of hTauT.
- Substrate-free and P4S-bound hTauT adopt an inward-open conformation, facilitating ion and substrate release.
- These findings improve understanding of substrate and ion recognition, aiding future drug development for TauT-related diseases.