Challenges and approaches to understand cholesterol-binding impact on membrane protein function: an NMR view.
Cell Mol Life Sci. 2018 Mar 08;:
Authors: Jaipuria G, Ukmar-Godec T, Zweckstetter M
Abstract
Experimental evidence for a direct role of lipids in determining the structure, dynamics, and function of membrane proteins leads to the term 'functional lipids'. In particular, the sterol molecule cholesterol modulates the activity of many membrane proteins. The precise nature of cholesterol-binding sites and the consequences of modulation of local membrane micro-viscosity by cholesterol, however, is often unknown. Here, we review the current knowledge of the interaction of cholesterol with transmembrane proteins, with a special focus on structural aspects of the interaction derived from nuclear magnetic resonance approaches. We highlight examples of the importance of cholesterol modulation of membrane protein function, discuss the specificity of cholesterol binding, and review the proposed binding motifs from a molecular perspective. We conclude with a short perspective on what could be future trends in research efforts targeted towards a better understanding of cholesterol/membrane protein interactions.
PMID: 29520423 [PubMed - as supplied by publisher]
Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR [Biophysics and Computational Biology]
Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR
Matthew R. Elkins, Jonathan K. Williams, Martin D. Gelenter, Peng Dai, Byungsu Kwon, Ivan V. Sergeyev, Bradley L. Pentelute, Mei Hong...
Date: 2017-12-05
The influenza M2 protein not only forms a proton channel but also mediates membrane scission in a cholesterol-dependent manner to cause virus budding and release. The atomic interaction of cholesterol with M2, as with most eukaryotic membrane proteins, has long been elusive. We have now determined the cholesterol-binding site of... Read More
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[NMR paper] Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.
Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.
Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.
Proc Natl Acad Sci U S A. 2017 Nov 20;:
Authors: Elkins MR, Williams JK, Gelenter MD, Dai P, Kwon B, Sergeyev IV, Pentelute BL, Hong M
Abstract
The influenza M2 protein not only forms a proton channel but also mediates membrane scission in a cholesterol-dependent manner to cause virus budding and release. The atomic interaction of cholesterol...
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11-22-2017 02:01 PM
[NMR paper] NMR Insight into Myosin-Binding Subunit Coiled Coil Structure Reveals Binding Interface with Protein Kinase G-I? Leucine Zipper in Vascular Function.
NMR Insight into Myosin-Binding Subunit Coiled Coil Structure Reveals Binding Interface with Protein Kinase G-I? Leucine Zipper in Vascular Function.
Related Articles NMR Insight into Myosin-Binding Subunit Coiled Coil Structure Reveals Binding Interface with Protein Kinase G-I? Leucine Zipper in Vascular Function.
J Biol Chem. 2017 Mar 09;:
Authors: Sharma AK, Birrane GG, Anklin C, Rigby AC, Alper SL
Abstract
Nitrovasodilators relax vascular smooth muscle cells (VSMC) in part by modulating the interaction of the C-terminal...
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03-11-2017 05:12 PM
[NMR paper] Micelles, Bicelles, and Nanodiscs: Comparing the Impact of Membrane Mimetics on Membrane Protein Backbone Dynamics
Micelles, Bicelles, and Nanodiscs: Comparing the Impact of Membrane Mimetics on Membrane Protein Backbone Dynamics
Detergents are often used to investigate the structure and dynamics of membrane proteins. Whereas the structural integrity seems to be preserved in detergents for many membrane proteins, their functional activity is frequently compromised, but can be restored in a lipid environment. Herein we show with per-residue resolution that while OmpX forms a stable ?-barrel in DPC detergent micelles, DHPC/DMPC bicelles, and DMPC nanodiscs, the pico- to nanosecond and micro- to...
A solution NMR view of protein dynamics in the biological membrane.
A solution NMR view of protein dynamics in the biological membrane.
A solution NMR view of protein dynamics in the biological membrane.
Curr Opin Struct Biol. 2011 Jul 30;
Authors: Chill JH, Naider F
Structure determination of membrane-associated proteins (MPs) represents a frontier of structural biology that is characterized by unique challenges in sample preparation and data acquisition. No less important is our ability to study the dynamics of MPs, since MP flexibility and characteristic motions often make sizeable contributions to their...
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08-03-2011 12:00 PM
[NMR paper] Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Related Articles Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Nat Struct Biol. 2001 Nov;8(11):926-31
Authors: Wand AJ
Recent developments in solution NMR methods have allowed for an unprecedented view of protein dynamics. Current insights into the nature of protein dynamics and their potential influence on protein structure, stability and function are reviewed. Particular emphasis is placed on the potential of fast side chain motion...
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[NMR paper] Solid-state NMR approaches for studying membrane protein structure.
Solid-state NMR approaches for studying membrane protein structure.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--arjournals.annualreviews.org-images-AnnualReviews100x25.gif Related Articles Solid-state NMR approaches for studying membrane protein structure.
Annu Rev Biophys Biomol Struct. 1992;21:25-47
Authors: Smith SO, Peersen OB
Challenges and approaches to understand cholesterol-binding impact on membrane protein function: an NMR view.
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