Cargando…

A partially-open inward-facing intermediate conformation of LeuT is associated with Na(+) release and substrate transport

Neurotransmitter:sodium symporters (NSS), targets of antidepressants and psychostimulants, clear neurotransmitters from the synaptic cleft through sodium (Na(+))-coupled transport. Substrate and Na(+) are thought to be transported from the extracellular to intracellular space through an alternating...

Descripción completa

Detalles Bibliográficos
Autores principales:	Terry, Daniel S., Kolster, Rachel A., Quick, Matthias, LeVine, Michael V., Khelashvili, George, Zhou, Zhou, Weinstein, Harel, Javitch, Jonathan A., Blanchard, Scott C.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Nature Publishing Group UK 2018
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5768729/ https://www.ncbi.nlm.nih.gov/pubmed/29335402 http://dx.doi.org/10.1038/s41467-017-02202-y

Ejemplares similares

X-ray structure of LeuT in an inward-facing occluded conformation reveals mechanism of substrate release
por: Gotfryd, Kamil, et al.
Publicado: (2020)

Role of Annular Lipids in the Functional Properties of Leucine Transporter LeuT Proteomicelles
por: LeVine, Michael V., et al.
Publicado: (2016)

The Membrane Protein LeuT in Micellar Systems: Aggregation Dynamics and Detergent Binding to the S2 Site
por: Khelashvili, George, et al.
Publicado: (2013)

Conformational dynamics of ligand-dependent alternating access in LeuT
por: Kazmier, Kelli, et al.
Publicado: (2014)

Experimental conditions can obscure the second high-affinity site in LeuT
por: Quick, Matthias, et al.
Publicado: (2012)

Crystal structures of LeuT reveal conformational dynamics in the outward-facing states
por: Fan, Jianjun, et al.
Publicado: (2021)

NbIT - A New Information Theory-Based Analysis of Allosteric Mechanisms Reveals Residues that Underlie Function in the Leucine Transporter LeuT
por: LeVine, Michael V., et al.
Publicado: (2014)

The allosteric mechanism of substrate-specific transport in SLC6 is mediated by a volumetric sensor
por: LeVine, Michael V., et al.
Publicado: (2019)

The Substrate-Driven Transition to an Inward-Facing Conformation in the Functional Mechanism of the Dopamine Transporter
por: Shan, Jufang, et al.
Publicado: (2011)

To be, or not to be two sites: that is the question about LeuT substrate binding
por: Reyes, Nicolas, et al.
Publicado: (2011)

The Amino Terminus of LeuT Changes Conformation in an Environment Sensitive Manner
por: Khan, Jawad A., et al.
Publicado: (2019)

Substrate-modulated unwinding of transmembrane helices in the NSS transporter LeuT
por: Merkle, Patrick S., et al.
Publicado: (2018)

A conserved leucine occupies the empty substrate site of LeuT in the Na(+)-free return state
por: Malinauskaite, Lina, et al.
Publicado: (2016)

The Environment Shapes the Inner Vestibule of LeuT
por: Sohail, Azmat, et al.
Publicado: (2016)

Substrate-modulated gating dynamics in a Na(+)-coupled neurotransmitter transporter homolog
por: Zhao, Yongfang, et al.
Publicado: (2011)

Direct assessment of substrate binding to the Neurotransmitter:Sodium Symporter LeuT by solid state NMR
por: Erlendsson, Simon, et al.
Publicado: (2017)

LRET-based intramolecular distance measurements in LeuT(Aa)
por: Sohail, Azmat, et al.
Publicado: (2011)

Neurotransmitter/sodium symporter orthologue LeuT has a single high–affinity substrate site
por: Piscitelli, Chayne L., et al.
Publicado: (2010)

Mechanism of the Association between Na(+) Binding and Conformations at the Intracellular Gate in Neurotransmitter:Sodium Symporters
por: Stolzenberg, Sebastian, et al.
Publicado: (2015)

Complete Mapping of Substrate Translocation Highlights the Role of LeuT N-terminal Segment in Regulating Transport Cycle
por: Cheng, Mary Hongying, et al.
Publicado: (2014)

Spontaneous Inward Opening of the Dopamine Transporter Is Triggered by PIP(2)-Regulated Dynamics of the N-Terminus
por: Khelashvili, George, et al.
Publicado: (2015)

Microseconds Simulations Reveal a New Sodium-binding Site and the Mechanism of Sodium-coupled Substrate Uptake by LeuT
por: Zomot, Elia, et al.
Publicado: (2015)

Locking Two Rigid-body Bundles in an Outward-Facing Conformation: The Ion-coupling Mechanism in a LeuT-fold Transporter
por: Li, Jing, et al.
Publicado: (2019)

A comparative study of structures and structural transitions of secondary transporters with the LeuT fold
por: Jeschke, Gunnar
Publicado: (2012)

Decrypting structural and functional changes in LeuT(Aa) at atomic level employing LRET
por: Sohail, Azmat, et al.
Publicado: (2012)

Resculpting the binding pocket of APC superfamily LeuT-fold amino acid transporters
por: Edwards, Noel, et al.
Publicado: (2017)

Shared dynamics of LeuT superfamily members and allosteric differentiation by structural irregularities and multimerization
por: Ponzoni, Luca, et al.
Publicado: (2018)

Structural Intermediates in a Model of the Substrate Translocation Path of the Bacterial Glutamate Transporter Homologue GltPh
por: Stolzenberg, Sebastian, et al.
Publicado: (2012)

A Functional Selectivity Mechanism at the Serotonin-2A GPCR Involves Ligand-Dependent Conformations of Intracellular Loop 2
por: Perez-Aguilar, Jose Manuel, et al.
Publicado: (2014)

Simulated annealing reveals the kinetic activity of SGLT1, a member of the LeuT structural family
por: Longpré, Jean-Philippe, et al.
Publicado: (2012)

Substrate-dependent proton antiport in neurotransmitter:sodium symporters
por: Zhao, Yongfang, et al.
Publicado: (2009)

Tabulature de leut
por: Ripa, Alberto da, d. 1551
Publicado: (1990)

Die leute auf Hemsö
por: Strindberg, August, 1849-1912
Publicado: (1890)

Unbiased Simulations Reveal the Inward-Facing Conformation of the Human Serotonin Transporter and Na(+) Ion Release
por: Koldsø, Heidi, et al.
Publicado: (2011)

Ligand-Dependent Conformations and Dynamics of the Serotonin 5-HT(2A) Receptor Determine Its Activation and Membrane-Driven Oligomerization Properties
por: Shan, Jufang, et al.
Publicado: (2012)

Single-molecule dynamics of gating in a neurotransmitter transporter homolog
por: Zhao, Yongfang, et al.
Publicado: (2010)

Metadynamics Simulations Reveal a Na(+) Independent Exiting Path of Galactose for the Inward-Facing Conformation of vSGLT
por: Bisha, Ina, et al.
Publicado: (2014)

Elucidating the Mechanism of Membrane Destabilization by the Preferred Modes of Insertion of the Sars-Cov2 Fusion Peptide
por: Khelashvili, George, et al.
Publicado: (2021)

AIM for Allostery: Using the Ising Model to Understand Information Processing and Transmission in Allosteric Biomolecular Systems
por: LeVine, Michael V., et al.
Publicado: (2015)

Junge Leute mit Zoster? – bei Lupus keine Seltenheit
Publicado: (2022)

Cannot write session to /tmp/vufind_sessions/sess_f607ib97lbvg26c60o1kqcdq5k