The LeuT-fold neurotransmitter:sodium symporter MhsT has two substrate sites

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Substrate and drug binding sites in LeuT.

LeuT is a member of the neurotransmitter/sodium symporter family, which includes the neuronal transporters for serotonin, norepinephrine, and dopamine. The original crystal structure of LeuT shows a primary leucine-binding site at the center of the protein. LeuT is inhibited by different classes of antidepressants that act as potent inhibitors of the serotonin transporter. The newly determined ...

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Direct assessment of substrate binding to the Neurotransmitter:Sodium Symporter LeuT by solid state NMR

The Neurotransmitter:Sodium Symporters (NSSs) represent an important class of proteins mediating sodium-dependent uptake of neurotransmitters from the extracellular space. The substrate binding stoichiometry of the bacterial NSS protein, LeuT, and thus the principal transport mechanism, has been heavily debated. Here we used solid state NMR to specifically characterize the bound leucine ligand ...

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To be, or not to be two sites: that is the question about LeuT substrate binding

Transport proteins of the neurotransmitter sodium symporter (NSS) family regulate the extracellular concentration of several neurotransmitters in the central nervous system. The only member of this family for which atomic-resolution structural data are available is the prokaryotic homologue LeuT. This protein has been used as a model system to study the molecular mechanism of transport of the N...

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Coupled global and local changes direct substrate translocation by neurotransmitter-sodium symporter ortholog LeuT.

Significant advances have been made in recent years in characterizing neurotransmitter:sodium symporter (NSS) family structure and function. Yet, many time-resolved events and intermediates that control the various stages of transport cycle remain to be elucidated. Whether NSSs harbor one or two sites for binding their substrates (neurotransmitters or amino acids), and what the role of the seco...

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Substrate binds in the S1 site of the F253A mutant of LeuT, a neurotransmitter sodium symporter homologue.

LeuT serves as the model protein for understanding the relationships between structure, mechanism and pharmacology in neurotransmitter sodium symporters (NSSs). At the present time, however, there is a vigorous debate over whether there is a single high-affinity substrate site (S1) located at the original, crystallographically determined substrate site or whether there are two high-affinity sub...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 2018

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.1717444115