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Merck

Recognition of Complex Core-Fucosylated N-Glycans by a Mini Lectin.

Angewandte Chemie (International ed. in English) (2018-06-30)
Aurore Cabanettes, Lukas Perkams, Carolina Spies, Carlo Unverzagt, Annabelle Varrot
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Biotinamidohexanoyl-6-aminohexanoic acid N-hydroxysuccinimide ester, ≥95% (TLC), powder
Sigma-Aldrich
Streptavidin−Peroxidase from Streptomyces avidinii, lyophilized powder
Sigma-Aldrich
SIGMAFAST OPD, tablet