Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
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Journal
IF	>30 >20 >10 >5 all

Title	Structural mechanism of substrate binding and inhibition of human taurine transporter.
Journal, issue, pages	Nat Commun, Year 2026
Publish date	Mar 20, 2026
Authors	Yuhan Qi / Ying Zhang / Duanning Wang / Jiameng Liu / Yue Zhou / Wenming Ji / Xinjing Chen / Luping Liu / Rui Wang / Jing-Xiang Wu /
PubMed Abstract	Taurine is a sulfur-containing amino acid that plays several crucial roles in the body. Its uptake is mediated by the taurine transporter (TauT). Genetic mutations and dysregulation of TauT have been ...Taurine is a sulfur-containing amino acid that plays several crucial roles in the body. Its uptake is mediated by the taurine transporter (TauT). Genetic mutations and dysregulation of TauT have been linked to various neurological disorders, cardiomyopathy, childhood progressive retinal degeneration, and cancer, making TauT a promising target for therapeutic intervention in these diseases. However, the structure and mechanism of TauT remain poorly understood. In this study, we present the structures of the human taurine transporter (hTauT) under four conditions: the substrate-free state, the taurine-bound state, the β-alanine-bound state, and the cyclic inhibitor piperidine-4-sulfonate (P4S)-bound state. These structures reveal that taurine binds at the central substrate-binding site of hTauT. Notably, β-alanine and the cyclic P4S inhibitors also mimic taurine, occupying the same substrate-binding site. In the substrate-free and P4S-bound forms, hTauT also adopt an inward-open conformation, where transmembrane helix TM1a bends toward the membrane, facilitating the opening of the intracellular gate for ion and substrate release. These structural insights enhance our understanding of the mechanisms underlying substrate and ion recognition and transport in hTauT, paving the way for the future development of taurine transporter substrate analogues or selective inhibitors.
External links	Nat Commun / PubMed:41857056
Methods	EM (single particle)
Resolution	2.69 - 3.33 Å
Structure data	62738 9l19 EMDB-62738, PDB-9l19: Structure of human apo Taurine Transporter in the inward-open conformation Method: EM (single particle) / Resolution: 3.33 Å 62739 9l1a EMDB-62739, PDB-9l1a: Structure of human apo Taurine Transporter in the inward-occluded conformation Method: EM (single particle) / Resolution: 2.75 Å 62740 9l1b EMDB-62740, PDB-9l1b: Structure of taurine-bound human Taurine Transporter in the inward-occluded conformation Method: EM (single particle) / Resolution: 2.9 Å 62741 9l1c EMDB-62741, PDB-9l1c: Structure of beta-alanine-bound human Taurine Transporter in the inward-occluded conformation Method: EM (single particle) / Resolution: 2.69 Å 62742 9l1d EMDB-62742, PDB-9l1d: Structure of piperidine-4-sulfonic acid-bound human Taurine Transporter in the inward-open conformation Method: EM (single particle) / Resolution: 3.24 Å 62743 9l1e EMDB-62743, PDB-9l1e: Structure of piperidine-4-sulfonic acid-bound human Taurine Transporter in the inward-occluded conformation Method: EM (single particle) / Resolution: 2.82 Å
Chemicals	ChemComp-Y01: CHOLESTEROL HEMISUCCINATE ChemComp-NA: Unknown entry ChemComp-CL: Unknown entry ChemComp-CLR: CHOLESTEROL ChemComp-HOH: WATER ChemComp-TAU: 2-AMINOETHANESULFONIC ACID ChemComp-BAL: BETA-ALANINE PDB-1ebd: DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED WITH THE BINDING DOMAIN OF THE DIHYDROLIPOAMIDE ACETYLASE
Source	homo sapiens (human)
Keywords	TRANSPORT PROTEIN / cancer / taurine / beta-alanine / piperidine-4-sulfonic acid