Related ArticlesStructural Analysis of CXCR4 - Antagonist Interactions Using Saturation-Transfer Double-Difference NMR.
Biochem Biophys Res Commun. 2015 Aug 21;
Authors: Cox BD, Mehta AK, DiRaddo JO, Liotta DC, Wilson LJ, Snyder JP
Abstract
CXCR4 is a GPCR involved in leukocyte trafficking. Small molecule antagonists of the receptor may treat inflammatory disease, cancer and HIV. Here we probe the binding of a tetrahydroisoquinoline-based antagonist (TIQ-10) to CXCR4 using saturation transfer double-difference (STDD) NMR. STDD spectra were acquired using extracts from Chinese Hamster Ovary cells expressing membrane-embedded CXCR4. The experiments demonstrate competitive binding between TIQ-10 and established antagonists and provide the TIQ-10 - CXCR4 binding epitope. Molecular modeling of TIQ-10 into the binding pocket provides a pose consistent with STDD-derived interactions. This study paves the way for future investigations of GPCR-ligand interactions in a biological milieu for use in chemical biology, biochemistry, structural biology, and rational drug design.
PMID: 26301631 [PubMed - as supplied by publisher]
[NMR paper] NMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
NMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR analysis of carbohydrate-binding interactions in solution: an approach using analysis of saturation transfer difference NMR spectroscopy.
Methods Mol Biol. 2014;1200:501-9
Authors: Hemmi H
Abstract
One of the most commonly used...
[NMR paper] Characterization of heparin-protein interaction by saturation transfer difference (STD) NMR.
Characterization of heparin-protein interaction by saturation transfer difference (STD) NMR.
Related Articles Characterization of heparin-protein interaction by saturation transfer difference (STD) NMR.
Anal Bioanal Chem. 2014 Mar 25;
Authors: Yu F, Roy S, Arevalo E, Schaeck J, Wang J, Holte K, Duffner J, Gunay NS, Capila I, Kaundinya GV
Abstract
The binding affinity and specificity of heparin to proteins is widely recognized to be sulfation-pattern dependent. However, for the majority of heparin-binding proteins (HBPs), it still remains...
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03-26-2014 12:44 PM
[NMR paper] Saturation transfer difference NMR for fragment screening.
Saturation transfer difference NMR for fragment screening.
Related Articles Saturation transfer difference NMR for fragment screening.
Curr Protoc Chem Biol. 2013 Dec 1;5(4):251-68
Authors: Begley DW, Moen SO, Pierce PG, Zartler ER
Abstract
Fragment screening by saturation transfer difference nuclear magnetic resonance (STD-NMR) is a robust method for identifying small molecule binders and is well suited to a broad set of biological targets. STD-NMR is exquisitely sensitive for detecting weakly binding compounds (a common characteristic of...
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01-07-2014 11:16 PM
[NMR paper] Specific RNA-protein interactions detected with saturation transfer difference NMR.
Specific RNA-protein interactions detected with saturation transfer difference NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.landesbioscience.com-icon-pubmed-Landesbioscience2.jpg Specific RNA-protein interactions detected with saturation transfer difference NMR.
RNA Biol. 2013 Jul 30;10(8)
Authors: Harris KA, Shekhtman A, Agris PF
Abstract
RNA, at the forefront of biochemical research due to its central role in biology, is recognized by proteins through various mechanisms. Analysis of the...
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08-21-2013 08:49 PM
[Question from NMRWiki Q&A forum] Saturation transfer difference TROSY
Saturation transfer difference TROSY
Has anyone added a pulse scheme for cross saturation to their TROSY for Bruker platform?
Could you share a pulse sequence if you have one?
Thanks!
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05-18-2013 09:22 AM
[NMR paper] Monomer-collagen interactions studied by saturation transfer difference NMR.
Monomer-collagen interactions studied by saturation transfer difference NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-sage.gif Related Articles Monomer-collagen interactions studied by saturation transfer difference NMR.
J Dent Res. 2013 Mar;92(3):284-8
Authors: Hiraishi N, Tochio N, Kigawa T, Otsuki M, Tagami J
Abstract
Functional monomers in dentin adhesives are involved in wetting dental substrates, demineralization, and the formation of calcium salts....
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04-09-2013 06:31 PM
[NMR paper] Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experim
Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase.
Related Articles Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase.
Proteins. 2004 Aug 1;56(2):346-53
Authors: Haselhorst T, Wilson JC, Thomson RJ, McAtamney S, Menting JG, Coppel RL, von Itzstein M
Saturation transfer difference...
Structural Analysis of CXCR4 - Antagonist Interactions Using Saturation-Transfer Double-Difference NMR.
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