Related ArticlesBinding 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 discover water channel activity modulators. However, inhibitors found so far are weak and/or lack specificity. For organic compounds, which lack of*high electron-dense atoms, the identification of binding sites is even more difficult. Nuclear magnetic resonance spectroscopy (NMR) requires large amounts of the protein, and expression and purification of mammalian aquaporins in large quantities is a difficult task. However, since aquaporin Z (AqpZ) can be purified and expressed in good quantities and has a high similarity to human AQP1 (~ 40% identity), it can be used as a model for studying the structure and function of human aquaporins. In the present study, we have used solid-state MAS NMR to investigate the binding of a lead compound [1-(4-methylphenyl)1H-pyrrole-2,5-dione] to AqpZ, through mapping of chemical shift perturbations in the presence of the compound.
PMID: 29916035 [PubMed - as supplied by publisher]
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] Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Timescales in an Archetypal Proton Channel - Insights from Solid-State NMR.
Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Timescales in an Archetypal Proton Channel - Insights from Solid-State NMR.
Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Timescales in an Archetypal Proton Channel - Insights from Solid-State NMR.
J Am Chem Soc. 2018 Jan 05;:
Authors: Mandala V, Gelenter MD, Hong M
Abstract
The influenza M2 protein forms a tetrameric proton channel that conducts protons from the acidic endosome into the virion by shuttling...
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01-06-2018 11:17 AM
HighField Solid-State NMR Spectroscopy Investigation of 15N-Labeled Rosette Nanotubes: Hydrogen Bond Network and Channel-Bound Water
HighField Solid-State NMR Spectroscopy Investigation of 15N-Labeled Rosette Nanotubes: Hydrogen Bond Network and Channel-Bound Water
Hicham Fenniri, Grigory A. Tikhomirov, Darren H. Brouwer, Souhaila Bouatra, Mounir El Bakkari, Zhimin Yan, Jae-Young Cho and Takeshi Yamazaki
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b02420/20160505/images/medium/ja-2016-02420c_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b02420
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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05-06-2016 03:39 AM
[NMR paper] TROSY NMR with a 52 kDa sugar transport protein and the binding of a small-molecule inhibitor.
TROSY NMR with a 52 kDa sugar transport protein and the binding of a small-molecule inhibitor.
Related Articles TROSY NMR with a 52 kDa sugar transport protein and the binding of a small-molecule inhibitor.
Mol Membr Biol. 2014 May 7;
Authors: Kalverda AP, Gowdy J, Thompson GS, Homans SW, Henderson PJ, Patching SG
Abstract
Abstract Using the sugar transport protein, GalP, from Escherichia coli, which is a homologue of human GLUT transporters, we have overcome the challenges for achieving high-resolution - and -methyl-TROSY NMR...
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05-09-2014 07:01 PM
Small-Molecule Binding Sites on Proteins Establishedby Paramagnetic NMR Spectroscopy
Small-Molecule Binding Sites on Proteins Establishedby Paramagnetic NMR Spectroscopy
Jia-Ying Guan, Peter H. J. Keizers, Wei-Min Liu, Frank Lo?hr, Simon P. Skinner, Edwin A. Heeneman, Harald Schwalbe, Marcellus Ubbink and Gregg Siegal
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja401323m/aop/images/medium/ja-2013-01323m_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja401323m
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/ZukfjIRmQq8
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04-05-2013 11:03 PM
[NMR paper] Small molecule binding sites on proteins established by paramagnetic NMR spectroscopy.
Small molecule binding sites on proteins established by paramagnetic NMR spectroscopy.
Related Articles Small molecule binding sites on proteins established by paramagnetic NMR spectroscopy.
J Am Chem Soc. 2013 Mar 20;
Authors: Guan JY, Keizers PH, Liu WM, Loehr F, Skinner SP, Heeneman EA, Schwalbe H, Ubbink M, Siegal GD
Abstract
Determining the three dimensional structure of a small molecule-protein complex with weak affinity can be a significant challenge. We present a paramagnetic NMR method to determine intermolecular structure...
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03-21-2013 02:58 PM
[NMR paper] NMR Methods for Detection of Small Molecule Binding to RGS4.
NMR Methods for Detection of Small Molecule Binding to RGS4.
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Methods Enzymol. 2013;522:133-52
Authors: Storaska AJ, Neubig RR
Abstract
The duration and amplitude of G-protein-coupled receptor (GPCR) signaling is controlled by regulator of G-protein signaling (RGS) proteins. The 20 RGS family members act as GTPase accelerating proteins through their interaction with the G? subunit of the G??? heterotrimer. Their influence over GPCR signaling has attracted many to...
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02-05-2013 09:51 PM
[NMR paper] NMR structure of a complex between MDM2 and a small molecule inhibitor.
NMR structure of a complex between MDM2 and a small molecule inhibitor.
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J Biomol NMR. 2004 Oct;30(2):163-73
Authors: Fry DC, Emerson SD, Palme S, Vu BT, Liu CM, Podlaski F
MDM2 is a regulator of cell growth processes that acts by binding to the tumor suppressor protein p53 and ultimately restraining its activity. While inactivation of p53 by mutation is commonly observed in human cancers, a substantial percentage of tumors express wild type p53. In many of...
Binding of a small molecule water channel inhibitor to aquaporin Z examined by solid-state MAS NMR.
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