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Lyann Sim, Magnus Groes, Kjeld Olesen and Anette Henriksen Structural and biochemical characterization of the N-terminal domain of flocculin Lg-Flo1p from Saccharomyces pastorianus reveals a unique specificity for phosphorylated mannose The FEBS Journal 280

Version of Record online: 24 JAN 2013 | DOI: 10.1111/febs.12102

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The crystal structure of the 25 kDa lectin domain of Lg–Flo1p flocculin from brewer's yeast was solved and its binding specificity towards oligosaccharides investigated. Lg-Flo1p has a 14-fold higher affinity for mannose-1-phosphate and glucose-1-phosphate, compared to their unphosphorylated counterparts. We propose that this higher affinity is due to charge interaction in a carbohydrate binding region unique to NewFlo type flocculins

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