Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 57, Issue 32, Pages 10178-10181Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201805165
Keywords
glycosylation; lectins; oligosaccharides; protein folding; structural biology
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Funding
- Horizon 2020 program of the European Union (iNEXT grant) [653706]
- French National Research Agency (Glyco@Alps grant) [ANR-15-IDEX-02]
- Deutsche Forschungsgemeinschaft [DFG: Un 63/4-2]
- French Ministry of Research
- Consortium for Functional Glycomics [GM62116]
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The mini fungal lectin PhoSL was recombinantly produced and characterized. Despite a length of only 40 amino acids, PhoSL exclusively recognizes N-glycans with 1,6-linked fucose. Core fucosylation influences the intrinsic properties and bioactivities of mammalian N-glycoproteins and its level is linked to various cancers. Thus, PhoSL serves as a promising tool for glycoprofiling. Without structural precedence, the crystal structure was solved using the zinc anomalous signal, and revealed an interlaced trimer creating a novel protein fold termed -prism III. Three biantennary core-fucosylated N-glycan azides of 8 to 12 sugars were cocrystallized with PhoSL. The resulting highly resolved structures gave a detailed view on how the exclusive recognition of 1,6-fucosylated N-glycans by such a small protein occurs. This work also provided a protein consensus motif for the observed specificity as well as a glimpse into N-glycan flexibility upon binding.
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