Substrate binds in the S1 site of the F253A mutant of LeuT, a neurotransmitter sodium symporter homologue
about
Nonclassical pharmacology of the dopamine transporter: atypical inhibitors, allosteric modulators, and partial substratesSpontaneous inward opening of the dopamine transporter is triggered by PIP2-regulated dynamics of the N-terminusStructural basis for action by diverse antidepressants on biogenic amine transportersDirect assessment of substrate binding to the Neurotransmitter:Sodium Symporter LeuT by solid state NMRComputational modeling of the N-terminus of the human dopamine transporter and its interaction with PIP2 -containing membranes.Microseconds simulations reveal a new sodium-binding site and the mechanism of sodium-coupled substrate uptake by LeuTNbIT--a new information theory-based analysis of allosteric mechanisms reveals residues that underlie function in the leucine transporter LeuT.Functional mechanisms of neurotransmitter transporters regulated by lipid-protein interactions of their terminal loops.Steric hindrance mutagenesis in the conserved extracellular vestibule impedes allosteric binding of antidepressants to the serotonin transporterChloride binding site of neurotransmitter sodium symporters.Coupled global and local changes direct substrate translocation by neurotransmitter-sodium symporter ortholog LeuT.The membrane protein LeuT in micellar systems: aggregation dynamics and detergent binding to the S2 site.SLC Transporters: Structure, Function, and Drug Discovery.Design and synthesis of 1-(3-(dimethylamino)propyl)-1-(4-fluorophenyl)-1,3-dihydroisobenzofuran-5-carbonitrile (citalopram) analogues as novel probes for the serotonin transporter S1 and S2 binding sites.Identification of novel serotonin transporter compounds by virtual screening.Chloride requirement for monoamine transportersImpact of disruption of secondary binding site S2 on dopamine transporter function.Biophysical Approaches to the Study of LeuT, a Prokaryotic Homolog of Neurotransmitter Sodium Symporters.Conformational Dynamics on the Extracellular Side of LeuT Controlled by Na+ and K+ Ions and the Protonation State of Glu290The aromatic and charge pairs of the thin extracellular gate of the γ-aminobutyric acid transporter GAT-1 are differently impacted by mutationLatch and trigger role for R445 in DAT transport explains molecular basis of DTDS.
P2860
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P2860
Substrate binds in the S1 site of the F253A mutant of LeuT, a neurotransmitter sodium symporter homologue
description
2012 nî lūn-bûn
@nan
2012 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Substrate binds in the S1 site ...... ter sodium symporter homologue
@ast
Substrate binds in the S1 site ...... ter sodium symporter homologue
@en
Substrate binds in the S1 site ...... ter sodium symporter homologue
@nl
type
label
Substrate binds in the S1 site ...... ter sodium symporter homologue
@ast
Substrate binds in the S1 site ...... ter sodium symporter homologue
@en
Substrate binds in the S1 site ...... ter sodium symporter homologue
@nl
prefLabel
Substrate binds in the S1 site ...... ter sodium symporter homologue
@ast
Substrate binds in the S1 site ...... ter sodium symporter homologue
@en
Substrate binds in the S1 site ...... ter sodium symporter homologue
@nl
P2860
P356
P1433
P1476
Substrate binds in the S1 site ...... ter sodium symporter homologue
@en
P2093
P2860
P356
10.1038/EMBOR.2012.110
P50
P577
2012-09-01T00:00:00Z