Recognition of Complex Core‐Fucosylated N‐Glycans by a Mini Lectin. Issue 32 (18th July 2018)

• Record Type: Journal Article
• Authors: Cabanettes, Aurore; Perkams, Lukas; Spies, Carolina; Unverzagt, Carlo; Varrot, Annabelle
• Is Part Of: Angewandte Chemie international edition. Volume 57:Issue 32(2018)
• Page Start: 10178
• Page End: 10181
• Publication Date: 2018-07-18
• Subjects: glycosylation -- lectins -- oligosaccharides -- protein folding -- structural biology; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201805165
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: The mini fungal lectin PhoSL was recombinantly produced and characterized. Despite a length of only 40 amino acids, PhoSL exclusively recognizes N‐glycans with α1, 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 β‐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 α1, 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. Abstract : Molecular prisms : The structure of rPhoSL unraveled a novel protein fold and the atomic basis for the exclusive recognition of α1, 6‐core‐fucosylated N‐glycans by a mini recombinant lectin. Thus, PhoSL serves as a promising tool for glycoprofiling.