Abstract
FGF-1 is a potent mitogen that, by interacting simultaneously with Heparan Sulfate Glycosaminoglycan HSGAG and the extracellular domains of its membrane receptor (FGFR), generates an intracellular signal that finally leads to cell division. The overall structure of the ternary complex Heparin:FGF-1:FGFR has been finally elucidated after some controversy and the interactions within the ternary complex have been deeply described. However, since the structure of the ternary complex was described, not much attention has been given to the molecular basis of the interaction between FGF-1 and the HSGAG. It is known that within the complex, the carbohydrate maintains the same helical structure of free heparin that leads to sulfate groups directed towards opposite directions along the molecular axis. The precise role of single individual interactions remains unclear, as sliding and/or rotating of the saccharide along the binding pocket are possibilities difficult to discard. The HSGAG binding pocket can be subdivided into two regions, the main one can accommodate a trisaccharide, while the other binds a disaccharide. We have studied and analyzed the interaction between FGF-1 and a library of trisaccharides by STD-NMR and selective longitudinal relaxation rates. The library of trisaccharides corresponds to the heparin backbone and it has been designed to interact with the main subsite of the protein.
[NMR paper] [Interactions between proteins and cation exchange adsorbents analyzed by NMR and hydrogen/deuterium exchange technique].
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Sheng Wu Gong Cheng Xue Bao. 2014 Sep;30(9):1454-63
Authors: Wang K, Hao D, Qi S, Ma G
Abstract
In silico acquirement of the accurate residue details of protein on chromatographic media is a bottleneck in protein chromatography separation and purification. Here we developed a novel approach by coupling with H/D exchange and nuclear magnetic resonance to observe hen egg white lysozyme (HEWL) unfolding behavior adsorbed on cation exchange media (SP Sepharose FF). Analysis of 1D 1H-NMR shows that protein unfolding accelerated...
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03-01-2015 12:18 PM
[NMR paper] NMR and computational methods in the structural and dynamic characterization of ligand-receptor interactions.
NMR and computational methods in the structural and dynamic characterization of ligand-receptor interactions.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR and computational methods in the structural and dynamic characterization of ligand-receptor interactions.
Adv Exp Med Biol. 2014;805:271-304
Authors: Ghitti M, Musco G, Spitaleri A
Abstract
The recurrent failures in drug discovery campaigns, the asymmetry between the...
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05-31-2014 01:47 AM
[NMR paper] Investigation of Lysine Side Chain Interactions of Interleukin-8 with Heparin and other Glycosaminoglycans Studied by a Methylation-NMR Approach.
Investigation of Lysine Side Chain Interactions of Interleukin-8 with Heparin and other Glycosaminoglycans Studied by a Methylation-NMR Approach.
Investigation of Lysine Side Chain Interactions of Interleukin-8 with Heparin and other Glycosaminoglycans Studied by a Methylation-NMR Approach.
Glycobiology. 2013 Aug 27;
Authors: Möbius K, Nordsieck K, Pichert A, Samsonov SA, Thomas L, Schiller J, Kalkhof S, Pisabarro MT, Beck-Sickinger AG, Huster D
Abstract
Although the interaction between interleukin-8 (IL-8) and glycosaminoglycans (GAG) is...
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08-29-2013 01:53 PM
NMR methods to monitor the enzymatic depolymerization of heparin.
NMR methods to monitor the enzymatic depolymerization of heparin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR methods to monitor the enzymatic depolymerization of heparin.
Anal Bioanal Chem. 2010 Sep 4;
Authors: Limtiaco JF, Beni S, Jones CJ, Langeslay DJ, Larive CK
Heparin and the related glycosaminoglycan, heparan sulfate, are polydisperse linear polysaccharides that mediate numerous biological processes due to their interaction with proteins....
[NMR paper] Characterization of tertiary interactions in a folded protein by NMR methods: studies
Characterization of tertiary interactions in a folded protein by NMR methods: studies of pH-induced structural changes in human growth hormone.
Related Articles Characterization of tertiary interactions in a folded protein by NMR methods: studies of pH-induced structural changes in human growth hormone.
Biochemistry. 1992 Sep 15;31(36):8587-96
Authors: Abildgaard F, Jørgensen AM, Led JJ, Christensen T, Jensen EB, Junker F, Dalbøge H
The pH-induced conformational changes in human growth hormone (hGH) have been studied, using a new...
Interactions between a Heparin Trisaccharide Library and FGF-1 Analyzed by NMR Methods.
Linear Mode
