ArticleNature structural & molecular biology2012
Structures of LeuT in bicelles define conformation and substrate binding in a membrane-like context.
Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
68 citing papers in PubMed, 111 citations in OpenAlex.
- Exploring the Structural Dynamics of LeuT Using EPR Spectroscopy: A Focus on Transmembrane Helix 10.Journal of neurochemistry · 2025Article
- Allosteric modulation of serotonin and dopamine transporters: New insights from computations and experiments.Current research in physiology · 2024Article
- Ins and Outs of Rocker Switch Mechanism in Major Facilitator Superfamily of Transporters.Membranes · 2023Review
- Taurine and Creatine Transporters as Potential Drug Targets in Cancer Therapy.International journal of molecular sciences · 2023Review
- Methods to study folding of alpha-helical membrane proteins in lipids.Open biology · 2022Review
- Mechanisms of membrane protein crystallization in 'bicelles'.Scientific reports · 2022Article
- Illumination of serotonin transporter mechanism and role of the allosteric site.Science advances · 2021Article
- Prokaryotic Solute/Sodium Symporters: Versatile Functions and Mechanisms of a Transporter Family.International journal of molecular sciences · 2021Review
- Identifying dynamic, partially occupied residues using anomalous scattering.Acta crystallographica. Section D, Structural biology · 2019Article
- Functional characterization of the alanine-serine-cysteine exchanger ofThe Journal of general physiology · 2019Article
- Structural, functional, and behavioral insights of dopamine dysfunction revealed by a deletion inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Clickable photoaffinity ligands for the human serotonin transporter based on the selective serotonin reuptake inhibitor (S)-citalopram.Bioorganic & medicinal chemistry letters · 2018Article
- Structural elements required for coupling ion and substrate transport in the neurotransmitter transporter homolog LeuT.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Transporters through the looking glass. An insight into the mechanisms of ion-coupled transport and methods that help reveal them.Journal of the Indian Institute of Science · 2018Article
- Flipped Phenyl Ring Orientations of Dopamine Binding with Human and Drosophila Dopamine Transporters: Remarkable Role of Three Nonconserved Residues.ACS chemical neuroscience · 2018Article
- Substrate-modulated unwinding of transmembrane helices in the NSS transporter LeuT.Science advances · 2018Article
- Lipid bilayer composition modulates the unfolding free energy of a knotted α-helical membrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Latch and trigger role for R445 in DAT transport explains molecular basis of DTDS.Bioorganic & medicinal chemistry letters · 2018Article
- Protonation state of glutamate 73 regulates the formation of a specific dimeric association of mVDAC1.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
8 more citing papers are in PubMed but not listed here.
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3 authors at 2 institutions in 1 country.
Funding
Abstract
Neurotransmitter sodium symporters (NSSs) catalyze the uptake of neurotransmitters into cells, terminating neurotransmission at chemical synapses. Consistent with the role of NSSs in the central nervous system, they are implicated in multiple diseases and disorders. LeuT, from Aquifex aeolicus, is a prokaryotic ortholog of the NSS family and has contributed to our understanding of the structure, mechanism and pharmacology of NSSs. At present, however, the functional state of LeuT in crystals grown in the presence of n-octyl-β-D-glucopyranoside (β-OG) and the number of substrate binding sites are controversial issues. Here we present crystal structures of LeuT grown in DMPC-CHAPSO bicelles and demonstrate that the conformations of LeuT-substrate complexes in lipid bicelles and in β-OG detergent micelles are nearly identical. Furthermore, using crystals grown in bicelles and the substrate leucine or the substrate analog selenomethionine, we find only a single substrate molecule in the primary binding site.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.