Structures of LeuT in bicelles define conformation and substrate binding in a membrane-like context
about
Visualizing functional motions of membrane transporters with molecular dynamics simulationsHow LeuT shapes our understanding of the mechanisms of sodium-coupled neurotransmitter transportersThe magic of bicelles lights up membrane protein structureSpontaneous inward opening of the dopamine transporter is triggered by PIP2-regulated dynamics of the N-terminusUnveiling the Mechanism of Arginine Transport through AdiC with Molecular Dynamics Simulations: The Guiding Role of Aromatic ResiduesSubstrate binds in the S1 site of the F253A mutant of LeuT, a neurotransmitter sodium symporter homologueStructural basis for action by diverse antidepressants on biogenic amine transportersStructural evidence for functional lipid interactions in the betaine transporter BetPThermostabilization of the Human Serotonin Transporter in an Antidepressant-Bound ConformationRole of Annular Lipids in the Functional Properties of Leucine Transporter LeuT ProteomicellesDirect assessment of substrate binding to the Neurotransmitter:Sodium Symporter LeuT by solid state NMRInsights from molecular dynamics: the binding site of cocaine in the dopamine transporter and permeation pathways of substrates in the leucine and dopamine transporters.Not just an oil slick: how the energetics of protein-membrane interactions impacts the function and organization of transmembrane proteins.Discovery of novel-scaffold monoamine transporter ligands via in silico screening with the S1 pocket of the serotonin transporterStructural dynamics of the monoamine transporter homolog LeuT from accelerated conformational sampling and channel analysisComputational and biochemical docking of the irreversible cocaine analog RTI 82 directly demonstrates ligand positioning in the dopamine transporter central substrate-binding site.Computational modeling of the N-terminus of the human dopamine transporter and its interaction with PIP2 -containing membranes.Identification of a second substrate-binding site in solute-sodium symporters.Microseconds simulations reveal a new sodium-binding site and the mechanism of sodium-coupled substrate uptake by LeuTAntagonist-induced conformational changes in dopamine transporter extracellular loop two involve residues in a potential salt bridgeMolecular mechanism of HIV-1 Tat interacting with human dopamine transporter.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 transporterThe cost of living in the membrane: a case study of hydrophobic mismatch for the multi-segment protein LeuT.Role of Histidine 547 of Human Dopamine Transporter in Molecular Interaction with HIV-1 Tat and Dopamine UptakeNanopharmacological Force Sensing to Reveal Allosteric Coupling in Transporter Binding SitesCoupled global and local changes direct substrate translocation by neurotransmitter-sodium symporter ortholog LeuT.When detergent meets bilayer: birth and coming of age of lipid bicelles.The membrane protein LeuT in micellar systems: aggregation dynamics and detergent binding to the S2 site.HIV-1 transgenic rats display an increase in [(3)H]dopamine uptake in the prefrontal cortex and striatum.Identification of novel serotonin transporter compounds by virtual screening.Protein and lipid interactions driving molecular mechanisms of in meso crystallization.Neurotransmitter transporters: structure meets function.New design strategies for antidepressant drugs.Membrane proteins, detergents and crystals: what is the state of the art?A comparative study of structures and structural transitions of secondary transporters with the LeuT fold.Crystallization of Membrane Proteins: An Overview.Computational modeling of human dopamine transporter structures, mechanism and its interaction with HIV-1 transactivator of transcription.Impact of disruption of secondary binding site S2 on dopamine transporter function.Conformational dynamics of a neurotransmitter:sodium symporter in a lipid bilayer.
P2860
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P2860
Structures of LeuT in bicelles define conformation and substrate binding in a membrane-like context
description
2012 nî lūn-bûn
@nan
2012 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունվարին 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
Structures of LeuT in bicelles ...... ing in a membrane-like context
@ast
Structures of LeuT in bicelles ...... ing in a membrane-like context
@en
Structures of LeuT in bicelles ...... ing in a membrane-like context
@nl
type
label
Structures of LeuT in bicelles ...... ing in a membrane-like context
@ast
Structures of LeuT in bicelles ...... ing in a membrane-like context
@en
Structures of LeuT in bicelles ...... ing in a membrane-like context
@nl
prefLabel
Structures of LeuT in bicelles ...... ing in a membrane-like context
@ast
Structures of LeuT in bicelles ...... ing in a membrane-like context
@en
Structures of LeuT in bicelles ...... ing in a membrane-like context
@nl
P2860
P3181
P356
P1476
Structures of LeuT in bicelles ...... ing in a membrane-like context
@en
P2093
Johannes Elferich
P2860
P2888
P3181
P356
10.1038/NSMB.2215
P50
P577
2012-01-15T00:00:00Z
P5875
P6179
1026435948