[NMR paper] Structure of the Functionally Important Extracellular Loop C of Human Aquaporin 1 Obtained by Solid-State NMR under Nearly Physiological Conditions.
Related ArticlesStructure of the Functionally Important Extracellular Loop C of Human Aquaporin 1 Obtained by Solid-State NMR under Nearly Physiological Conditions.
J Phys Chem B. 2019 09 12;123(36):7700-7710
Authors: Dingwell DA, Brown LS, Ladizhansky V
Abstract
Human aquaporin 1 (hAQP1) is the first discovered selective water channel present in lipid membranes of multiple types of cells. Several structures of hAQP1 and its bovine homolog have been obtained by electron microscopy and X-ray crystallography, giving a consistent picture of the transmembrane domain with the water-conducting pore. The transmembrane domain is formed by six full helices and two half-helices, which form a central constriction with conserved asparagine-proline-alanine motifs. Another constriction, the aromatic/arginine (ar/R) filter, is found close to the extracellular surface, and includes aromatic residues and a conserved arginine (Arg-195). Although the existing crystal structures largely converge on the location of helical segments, they differ in details of conformation of the longest extracellular loop C and its interactions with the ar/R filter (in particular, with Arg-195). Here, we use solid-state nuclear magnetic resonance to determine multiple interatomic distances, and come up with a refined structural model for hAQP1, which represents a physiologically relevant state predominant at noncryogenic temperatures in a lipid environment. The model clearly disambiguates the position of the Arg-195 sidechain disputed previously and shows a number of interactions for loop C, both with the ar/R filter and a number of other residues on the extracellular side of hAQP1.
[NMR paper] Improved Protocol for the Production of the Low-Expression Eukaryotic Membrane Protein Human Aquaporin 2 in Pichia pastoris for Solid-State NMR.
Improved Protocol for the Production of the Low-Expression Eukaryotic Membrane Protein Human Aquaporin 2 in Pichia pastoris for Solid-State NMR.
Related Articles Improved Protocol for the Production of the Low-Expression Eukaryotic Membrane Protein Human Aquaporin 2 in Pichia pastoris for Solid-State NMR.
Biomolecules. 2020 Mar 11;10(3):
Authors: Munro R, de Vlugt J, Ladizhansky V, Brown LS
Abstract
Solid-state nuclear magnetic resonance (SSNMR) is a powerful biophysical technique for studies of membrane proteins; it requires the...
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[NMR paper] Binding of a small molecule water channel inhibitor to aquaporin Z examined by solid-state MAS NMR.
Binding of a small molecule water channel inhibitor to aquaporin Z examined by solid-state MAS NMR.
Related Articles Binding of a small molecule water channel inhibitor to aquaporin Z examined by solid-state MAS NMR.
J Biomol NMR. 2018 Jun 18;:
Authors: Phillips M, To J, Yamazaki T, Nagashima T, Torres J, Pervushin K
Abstract
Aquaporins are integral membrane proteins that facilitate water flow across biological membranes. Their involvement in multiple physiological functions and disease states has prompted intense research to...
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06-20-2018 08:56 PM
Binding of a small molecule water channel inhibitor to aquaporin Z examined by solid-state MAS NMR
Binding of a small molecule water channel inhibitor to aquaporin Z examined by solid-state MAS NMR
Abstract
Aquaporins are integral membrane proteins that facilitate water flow across biological membranes. Their involvement in multiple physiological functions and disease states has prompted intense research to discover water channel activity modulators. However, inhibitors found so far are weak and/or lack specificity. For organic compounds, which lack ofÂ*high electron-dense atoms, the identification of binding sites is even more difficult. Nuclear...
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06-18-2018 10:45 AM
[NMR paper] Structure and Dynamics of Extracellular Loops in Human Aquaporin-1 from Solid-State NMR and Molecular Dynamics.
Structure and Dynamics of Extracellular Loops in Human Aquaporin-1 from Solid-State NMR and Molecular Dynamics.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Structure and Dynamics of Extracellular Loops in Human Aquaporin-1 from Solid-State NMR and Molecular Dynamics.
J Phys Chem B. 2016 09 22;120(37):9887-902
Authors: Wang S, Ing C, Emami S, Jiang Y, Liang H, Pomès R, Brown LS, Ladizhansky V
Abstract
Multiple moderate-resolution crystal structures...
[NMR paper] NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions.
NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions.
Related Articles NMR Spectroscopic Studies of Intrinsically Disordered Proteins at Near-Physiological Conditions.
Angew Chem Int Ed Engl. 2013 Sep 20;
Authors: Gil S, Hošek T, Solyom Z, Kümmerle R, Brutscher B, Pierattelli R, Felli IC
Abstract
When approaching physiological conditions, solvent exchange of amide protons in intrinsically disordered proteins (IDPs) is so pronounced that it becomes a key feature to be considered in NMR experiment...
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10-12-2013 05:24 PM
[NMR paper] Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra.
Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra.
J Biomol NMR. 2013 Jan 24;
Authors: Emami S, Fan Y, Munro R, Ladizhansky V, Brown LS
Abstract
One of the biggest challenges in solid-state NMR studies of membrane proteins is to obtain a...
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02-03-2013 10:19 AM
The NMR solution structure of human epidermal growth factor (hEGF) at physiological pH and its interactions with suramin.
The NMR solution structure of human epidermal growth factor (hEGF) at physiological pH and its interactions with suramin.
The NMR solution structure of human epidermal growth factor (hEGF) at physiological pH and its interactions with suramin.
Biochem Biophys Res Commun. 2010 Nov 26;402(4):705-10
Authors: Huang HW, Mohan SK, Yu C
Human epidermal growth factor (hEGF) induces the proliferation, differentiation and survival of various cell types including tumor-derived cells. Generally, hEGF performs its biological function by binding to a specific...
Structure of the Functionally Important Extracellular Loop C of Human Aquaporin 1 Obtained by Solid-State NMR under Nearly Physiological Conditions.
Linear Mode
