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A lectin from the Chinese bird-hunting spider binds sialic acids

AuthorsSiebert, Hans-Christian; Lu, Shan-Yun; Wechselberger, Rainer; Born, Karin; Eckert, Thomas; Liang, Songping; von der Lieth, Claus-Wilhelm; Jiménez-Barbero, Jesús ; Schauer, Roland; Vliegenthart, Johannes F.G.; Lütteke, Thomas; Kožár, Tibor
KeywordsSialic acid
Carbohydrate–protein interaction
Molecular modeling
NMR analysis
Issue DateAug-2009
CitationCarbohydrate Research 344(12):1515-25(2009)
AbstractThe affinity to sialic acid-containing oligosaccharides of the small-animal lectin SHL-I isolated from the venom of the Chinese bird-hunting spider Selenocosmia huwena is here described for the first time. By a strategic combination of NMR techniques, molecular modeling, and data mining tools it was possible to identify the crucial amino acid residues that are responsible for SHL-I’s ability to bind sialic acid residues in a specific way. Furthermore, we are able to discuss the role of the functional groups of sialic acid when bound to SHL-I. Also the impact of Pro31 in its cis- or trans-form on SHL-I’s ligand affinity is of special interest, since it answers the question if Trp32 is a crucial amino acid for stabilizing complexes between SHL-I and sialic acid. SHL-I can be considered as a proper model system that provides further insights into the binding mechanisms of small-animal lectins to sialic acid on a sub-molecular level
Description12 páginas, 7 figuras, 1 tabla, 2 figuras suplementarias -- PAGS nros. 1515-1525
Publisher version (URL)http://dx.doi.org/10.1016/j.carres.2009.06.002
Appears in Collections:(CIB) Artículos
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