Ion-controlled conformational dynamics in the outward-open transition from an occluded state of LeuT. - Wikidata - wikimedia - TriplyDB

Ion-controlled conformational dynamics in the outward-open transition from an occluded state of LeuT.

Ion-controlled conformational dynamics in the outward-open transition from an occluded state of LeuT.

http://www.wikidata.org/entity/Q36208010

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Visualizing functional motions of membrane transporters with molecular dynamics simulations Spontaneous inward opening of the dopamine transporter is triggered by PIP2-regulated dynamics of the N-terminus A conserved leucine occupies the empty substrate site of LeuT in the Na(+)-free return state.Substrate-bound outward-open state of the betaine transporter BetP provides insights into Na+ coupling.Role of Annular Lipids in the Functional Properties of Leucine Transporter LeuT Proteomicelles Conformational Changes in Two Inter-Helical Loops of Mhp1 Membrane Transporter.Hydrophobic plug functions as a gate in voltage-gated proton channels.Missense dopamine transporter mutations associate with adult parkinsonism and ADHD.An N-terminal threonine mutation produces an efflux-favorable, sodium-primed conformation of the human dopamine transporter Structural dynamics of the monoamine transporter homolog LeuT from accelerated conformational sampling and channel analysis Conformational cycle and ion-coupling mechanism of the Na+/hydantoin transporter Mhp1.Computational 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.Metadynamics simulations reveal a Na+ independent exiting path of galactose for the inward-facing conformation of vSGLT Microseconds simulations reveal a new sodium-binding site and the mechanism of sodium-coupled substrate uptake by LeuT The molecular mechanism of ion-dependent gating in secondary transporters.Mapping the gating and permeation pathways in the voltage-gated proton channel Hv1.Mechanism of the Association between Na+ Binding and Conformations at the Intracellular Gate in Neurotransmitter:Sodium Symporters Computational characterization of structural dynamics underlying function in active membrane transporters.Functional mechanisms of neurotransmitter transporters regulated by lipid-protein interactions of their terminal loops.The Environment Shapes the Inner Vestibule of LeuT.AIM for Allostery: Using the Ising Model to Understand Information Processing and Transmission in Allosteric Biomolecular Systems.Two Na+ Sites Control Conformational Change in a Neurotransmitter Transporter Homolog Chloride binding site of neurotransmitter sodium symporters.Computational approaches to detect allosteric pathways in transmembrane molecular machines.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.Na+ coordination at the Na2 site of the Na+/I- symporter.Functional identification and characterization of sodium binding sites in Na symporters.The two Na+ sites in the human serotonin transporter play distinct roles in the ion coupling and electrogenicity of transport A Markov State-based Quantitative Kinetic Model of Sodium Release from the Dopamine Transporter.How does water pass through a sugar transporter?Conformational dynamics of a neurotransmitter:sodium symporter in a lipid bilayer.The Sodium/Iodide Symporter (NIS): Molecular Physiology and Preclinical and Clinical Applications.Ion channels and ion selectivity.MHC class II complexes sample intermediate states along the peptide exchange pathway.Conformational Dynamics on the Extracellular Side of LeuT Controlled by Na+ and K+ Ions and the Protonation State of Glu290 Structure and Dynamics Study of LeuT Using the Markov State Model and Perturbation Response Scanning Reveals Distinct Ion Induced Conformational States.Insights on Na(+) binding and conformational dynamics in multidrug and toxic compound extrusion transporter NorM.Mechanism of Substrate Translocation in an Alternating Access Transporter.

P2860

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P2860

Ion-controlled conformational dynamics in the outward-open transition from an occluded state of LeuT.

http://www.wikidata.org/entity/Q36208010

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年论文

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Ion-controlled conformational ...... rom an occluded state of LeuT.

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Ion-controlled conformational ...... rom an occluded state of LeuT.

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Ion-controlled conformational ...... rom an occluded state of LeuT.

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Ion-controlled conformational ...... rom an occluded state of LeuT.

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Ion-controlled conformational ...... rom an occluded state of LeuT.

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J.BPJ.2012.07.044

P1433

Biophysical Journal

P1476

Ion-controlled conformational ...... rom an occluded state of LeuT.

@en

P2093

Chunfeng Zhao

http://www.w3.org/2001/XMLSchema#string

Harel Weinstein

http://www.w3.org/2001/XMLSchema#string

Lei Shi

http://www.w3.org/2001/XMLSchema#string

Luis Gracia

http://www.w3.org/2001/XMLSchema#string

Sebastian Stolzenberg

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Sergei Noskov

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P2860

Gaussian-weighted RMSD superposition of proteins: a structural comparison for flexible proteins and predicted protein structures.

CHARMM: the biomolecular simulation program

A competitive inhibitor traps LeuT in an open-to-out conformation.

X-ray structures of LeuT in substrate-free outward-open and apo inward-open states

VMD: visual molecular dynamics

Scalable molecular dynamics with NAMD

Crystal structure of a bacterial homologue of Na+/Cl--dependent neurotransmitter transporters

Substrate-dependent proton antiport in neurotransmitter:sodium symporters.

Ion/substrate-dependent conformational dynamics of a bacterial homolog of neurotransmitter:sodium symporters.

Single-molecule dynamics of gating in a neurotransmitter transporter homologue

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878-888

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10.1016/J.BPJ.2012.07.044

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5

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103

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3433624

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