Neurotransmitter:sodium symporters (NSS) reuptake neurotransmitter molecules from the synaptic space through Na^(+)-coupled transport. They are thought to work via the alternating access mechanism, exploring multiple configurations dictated by the binding of substrates and ions. Much of the current knowledge about these transporters has been derived from examining the structure of the Leucine Transporter (LeuT), a bacterial counterpart to human NSSs. Multiple crystal structures of LeuT provided...
[NMR paper] Solution NMR Backbone Assignment of the C-Terminal Region of Human Dynein Light Intermediate Chain 2 (LIC2-C) Unveils Structural Resemblance with Its Homologue LIC1-C
Solution NMR Backbone Assignment of the C-Terminal Region of Human Dynein Light Intermediate Chain 2 (LIC2-C) Unveils Structural Resemblance with Its Homologue LIC1-C
Dynein, a homodimeric protein complex, plays a pivotal role in retrograde transportation along microtubules within cells. It consists of various subunits, among which the light intermediate chain (LIC) performs diverse functions, including cargo adaptor binding. In contrast to the vertebrate LIC homolog LIC1, LIC2 has received relatively limited characterization thus far, despite partially orthogonal functional roles. In this...
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07-21-2023 11:06 AM
[NMR paper] Direct assessment of substrate binding to the Neurotransmitter:Sodium Symporter LeuT by solid state NMR.
Direct assessment of substrate binding to the Neurotransmitter:Sodium Symporter LeuT by solid state NMR.
Direct assessment of substrate binding to the Neurotransmitter:Sodium Symporter LeuT by solid state NMR.
Elife. 2017 Jan 24;6:
Authors: Erlendsson S, Gotfryd K, Larsen FH, Mortensen JS, Geiger MA, van Rossum BJ, Oschkinat H, Gether U, Teilum K, Loland CJ
Abstract
The Neurotransmitter:Sodium Symporters (NSSs) represent an important class of proteins mediating sodium-dependent uptake of neurotransmitters from the extracellular...
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01-25-2017 11:13 AM
[NMR paper] Antigenic peptide recognition on the human ABC transporter TAP resolved by DNP-enhanced solid-state NMR spectroscopy.
Antigenic peptide recognition on the human ABC transporter TAP resolved by DNP-enhanced solid-state NMR spectroscopy.
Related Articles Antigenic peptide recognition on the human ABC transporter TAP resolved by DNP-enhanced solid-state NMR spectroscopy.
J Am Chem Soc. 2016 Sep 23;
Authors: Lehnert E, Mao J, Mehdipour AR, Hummer G, Abele R, Glaubitz C, Tampé R
Abstract
The human transporter associated with antigen processing (TAP) is a 140-kDa heterodimeric ABC transport complex, which selects peptides for export into the...
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09-24-2016 05:20 PM
[NMR paper] Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy.
Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy.
Ligand-Induced Conformational Changes of the Multidrug Resistance Transporter EmrE Probed by Oriented Solid-State NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Aug 12;
Authors: Gayen A, Banigan JR, Traaseth NJ
Abstract
An EmrE-ging market: Oriented solid-state NMR spectroscopy and biochemical cross-linking experiments were used to show that the ligand-free membrane protein transporter EmrE forms...
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08-14-2013 05:24 PM
[NMR paper] Structural Elucidation of Transmembrane Transporter Protein Bilitranslocase: Conformational analysis of the second transmembrane region TM2 by molecular dynamics and NMR spectroscopy.
Structural Elucidation of Transmembrane Transporter Protein Bilitranslocase: Conformational analysis of the second transmembrane region TM2 by molecular dynamics and NMR spectroscopy.
Related Articles Structural Elucidation of Transmembrane Transporter Protein Bilitranslocase: Conformational analysis of the second transmembrane region TM2 by molecular dynamics and NMR spectroscopy.
Biochim Biophys Acta. 2013 Jun 14;
Authors: Choudhury AR, Perdih A, Zuperl S, Sikorska E, Solmajer T, Jurga S, Zhukov I, Novi? M
Abstract
Membrane proteins...
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06-19-2013 08:55 PM
Structural Elucidation of Transmembrane Transporter Protein Bilitranslocase: Conformational analysis of the second transmembrane region TM2 by molecular dynamics and NMR spectroscopy
Structural Elucidation of Transmembrane Transporter Protein Bilitranslocase: Conformational analysis of the second transmembrane region TM2 by molecular dynamics and NMR spectroscopy
Publication date: Available online 14 June 2013
Source:Biochimica et Biophysica Acta (BBA) - Biomembranes</br>
Author(s): Amrita Roy Choudhury , Andrej Perdih , Špela Župerl , Emilia Sikorska , Tom Solmajer , Stefan Jurga , Igor Zhukov , Marjana Novi?</br>
Membrane proteins represent about a third of the gene products in most organisms, as revealed by the genome sequencing...
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06-15-2013 08:18 AM
Unravelling the Conformational Plasticity of the Extracellular Domain of a Prokaryotic nAChR Homologue in Solution by NMR
Unravelling the Conformational Plasticity of the Extracellular Domain of a Prokaryotic nAChR Homologue in Solution by NMR
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi201223u/aop/images/medium/bi-2011-01223u_0002.gif
Biochemistry
DOI: 10.1021/bi201223u
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/rGTPGWIkyp0
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Monitoring conformational changes in the human neurotransmitter transporter homologue LeuT with (19)F-NMR spectroscopy
Linear Mode
