Cryo-EM structure of apo human SLC19A3 in outward-open state
Ontology highlight
ABSTRACT:
SUBMITTER: Florian Gabriel
PROVIDER: EMPIAR-12467 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural basis of thiamine transport and drug recognition by SLC19A3.
Gabriel Florian F Spriestersbach Lea L Fuhrmann Antonia A Jungnickel Katharina E J KEJ Mostafavi Siavash S Pardon Els E Steyaert Jan J Löw Christian C
Nature communications 20241002 1
Thiamine (vitamin B<sub>1</sub>) functions as an essential coenzyme in cells. Humans and other mammals cannot synthesise this vitamin de novo and thus have to take it up from their diet. Eventually, every cell needs to import thiamine across its plasma membrane, which is mainly mediated by the two specific thiamine transporters SLC19A2 and SLC19A3. Loss of function mutations in either of these transporters lead to detrimental, life-threatening metabolic disorders. SLC19A3 is furthermore a major ...[more]
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