NMR and Molecular Recognition of N-Glycans: Remote Modifications of the Saccharide Chain Modulate Binding Features.
ACS Chem Biol. 2017 Feb 13;:
Authors: Gimeno A, Reichardt NC, Cañada FJ, Perkams L, Unverzagt C, Jimenez-Barbero J, Arda A
Abstract
Glycans play a key role as recognition elements in the communication of cells and other organisms. Thus, the analysis of carbohydrate-protein interactions has gained significant importance. In particular, Nuclear Magnetic Resonance (NMR) techniques are considered powerful tools to detect relevant features in the interaction between sugars and their natural receptors. Here we present the results obtained in the study on the molecular recognition of different mannose-containing glycans by Pisum Sativum Agglutinin. NMR experiments supported by Corcema-ST analysis, Isothermal Titration Calorimetry (ITC) experiments and Molecular Dynamics (MD) protocols have been successfully applied to unmask important binding features and especially to determine how a remote branching substituent significantly alters the binding mode of the sugar entity. These results highlight the key influence of common structural modifications in natural glycans on molecular recognition processes, and underscore their importance for the development of biomedical applications.
PMID: 28192664 [PubMed - as supplied by publisher]
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Abstract
The FGLamide...
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J Phys Chem B. 2013 Mar 26;
Authors: Battistel MD, Pendrill R, Widmalm G, Freedberg DI
Abstract
With this report we introduce the abundant hydroxyl groups of glycans as NMR handles and structural probes that expand the repertoire of tools for structure-function studies on glycans in...
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Molecular Recognitionof Complex-Type Biantennary N-Glycans by ProteinReceptors: a Three-DimensionalView on Epitope Selection by NMR
Molecular Recognitionof Complex-Type Biantennary N-Glycans by ProteinReceptors: a Three-DimensionalView on Epitope Selection by NMR
Ana Arda?, Pilar Blasco, Daniel Varo?n Silva, Volker Schubert, Sabine Andre?, Marta Bruix, F. Javier Can?ada, Hans-Joachim Gabius, Carlo Unverzagt and Jesu?s Jime?nez-Barbero
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja3104928/aop/images/medium/ja-2012-104928_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/ja3104928
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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[NMR paper] Molecular recognition of complex-type biantennary N-glycans by protein receptors: a 3D view on epitope selection by NMR.
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Molecular recognition of complex-type biantennary N-glycans by protein receptors: a 3D view on epitope selection by NMR.
J Am Chem Soc. 2013 Jan 29;
Authors: Arda A, Blasco P, Varon Silva D, Schubert V, André S, Bruix M, Cañada FJ, Gabius HJ, Unverzagt C, Jimenez-Barbero J
Abstract
The current surge in defining...
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Biomol NMR Assign. 2013 Jan 22;
Authors: Orbán-Németh Z, Henen MA, Geist L, Zerko S, Saxena S, Stanek J, Ko?mi?ski W, Propst F, Konrat R
Abstract
Microtubule-associated protein 1B (MAP1B) is a classical...
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Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2139-44
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[NMR paper] Structural features of the binding site for ribosomal protein S8 in Escherichia coli
Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy.
Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2139-44
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