Related ArticlesNMR study of short ?(1-3)-glucans provides insights into the structure and interaction with Dectin-1.
Glycoconj J. 2013 Nov 29;
Authors: Hanashima S, Ikeda A, Tanaka H, Adachi Y, Ohno N, Takahashi T, Yamaguchi Y
Abstract
?(1-3)-Glucans, abundant in fungi, have the potential to activate the innate immune response against various pathogens. Although part of the action is exerted through the C-type lectin-like receptor Dectin-1, details of the interaction mechanism with respect to glucan chain-length remain unclear. In this study, we investigated a set of short ?(1-3)-glucans with varying degree of polymerization (DP); 3, 6, 7, 16, and laminarin (average DP; 25), analyzing the relationship between the structure and interaction with the C-type lectin-like domain (CTLD) of Dectin-1. The interaction of short ?(1-3)-glucans (DP6, DP16, and laminarin) with the CTLD of Dectin-1 was systematically analyzed by (1)H-NMR titration as well as by saturation transfer difference (STD)-NMR. The domain interacted weakly with DP6, moderately with DP16 and strongly with laminarin, the latter plausibly forming oligomeric protein-laminarin complexes. To obtain structural insights of short ?(1-3)-glucans, the exchange rates of hydroxy protons were analyzed by deuterium induced (13)C-NMR isotope shifts. The hydroxy proton at C4 of laminarin has slower exchange with the solvent than those of DP7 and DP16, suggesting that laminarin has a secondary structure. Diffusion ordered spectroscopy revealed that none of the short ?(1-3)-glucans including laminarin forms a double or triple helix in water. Insights into the interaction of the short ?(1-3)-glucans with Dectin-1 CTLD provide a basis to understand the molecular mechanisms of ?-glucan recognition and cellular activation by Dectin-1.
PMID: 24293021 [PubMed - as supplied by publisher]
[NMR paper] pH-Independence of trialanine and the effects of termini blocking in short peptides: a combined vibrational, NMR, UVCD, and molecular dynamics study.
pH-Independence of trialanine and the effects of termini blocking in short peptides: a combined vibrational, NMR, UVCD, and molecular dynamics study.
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J Phys Chem B. 2013 Apr 11;117(14):3689-706
Authors: Toal S, Meral D, Verbaro D, Urbanc B, Schweitzer-Stenner R
Abstract...
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[NMR paper] 1H NMR study on the short- and long-term impact of two training programs of sprint running on the metabolic fingerprint of human serum.
1H NMR study on the short- and long-term impact of two training programs of sprint running on the metabolic fingerprint of human serum.
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J Proteome Res. 2013 Jan 4;12(1):470-80
Authors: Pechlivanis A, Kostidis S, Saraslanidis P, Petridou A, Tsalis G, Veselkov K, Mikros E, Mougios V, Theodoridis GA...
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[NMR paper] Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils.
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Annu Rev Biophys. 2013 Mar 22;
Authors: Comellas G, Rienstra CM
Abstract
Protein structure determination methods using magic-angle spinning solidstate nuclear magnetic resonance (MAS SSNMR) have experienced a remarkable...
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17O NMR Gives Unprecedented Insights into the Structure of Supported Catalysts and Their Interaction with the Silica Carrier
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Nicolas Merle, Julien Tre?bosc, Anne Baudouin, Iker Del Rosal, Laurent Maron, Kai Szeto, Marie Genelot, Andre? Mortreux, Mostafa Taoufik, Laurent Delevoye and Re?gis M. Gauvin
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja301085m/aop/images/medium/ja-2012-01085m_0017.gif
Journal of the American Chemical Society
DOI: 10.1021/ja301085m
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Nucleic Acids Res. 2003 Aug 15;31(16):4747-54
Authors: Lee JH, Park CJ, Arunkumar...
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[NMR paper] Secondary structure and zinc ligation of human recombinant short-form stromelysin by
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Biochemistry. 1993 Dec 7;32(48):13098-108
Authors: Gooley PR, Johnson BA, Marcy AI, Cuca GC, Salowe SP, Hagmann WK, Esser CK, Springer JP
Stromelysin-1, a member of the matrix metalloendoprotease family, is a zinc protease involved in the degradation of connective tissue in the...
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[NMR paper] Short chain phospholipids in membrane protein crystallization: a 31P-NMR study of col
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Chem Phys Lipids. 1990 Sep;55(3):351-4
Authors: Eisele JL, Neumann JM, Chachaty C
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