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Publication Abstract from PubMed

We recombinantly produced and characterized the mini fungal lectin PhoSL. Despite a length of only 40 amino acids, PhoSL exclusively recognizes N-glycans with beta1,6-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, we solved its crystal structure using the zinc anomalous signal. We revealed an interlaced trimer creating a novel protein fold termed beta-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 alpha1,6-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 on N-glycan flexibility upon binding.

Recognition of complex core fucosylated N-glycans by a mini lectin.,Cabanettes A, Perkams L, Spies C, Unverzagt C, Varrot A Angew Chem Int Ed Engl. 2018 Jun 29. doi: 10.1002/anie.201805165. PMID:29956878^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.