Structural highlights
Publication Abstract from PubMedThe core alpha1-6 fucosylation-specific lectin from a mushroom Pholiota squarrosa (PhoSL) is a potential tool for precise diagnosis of cancers. This lectin consists of only 40 amino acids and can be chemically synthesized. We showed here that a synthesized PhoSL peptide formed a trimer by gel filtration and chemical cross-linking assays, and determined a structure of the PhoSL trimer by NMR. The structure possesses a beta-prism motif with a three-fold rotational symmetry, where three antiparallel beta-sheets are tightly connected by swapping of beta-strands. A triad of Trp residues comprises the structural core, forming NH-pi electrostatic interactions among the indole rings. NMR analysis with an excess amount of fucose revealed the structural basis for the molecular recognition. Namely, fucose deeply enters a pocket formed at a junction of beta-sheet edges, with the methyl group placed at the bottom. It forms a number of hydrophobic and hydrogen-bonding interactions with PhoSL residues. In spite of partial similarities to the structures of other functionally related lectins, the arrangement of the antiparallel beta-sheets in the PhoSL trimer is novel as a structural scaffold, and thus defines a novel type of lectin structure. The trimeric solution structure and fucose-binding mechanism of the core fucosylation-specific lectin PhoSL.,Yamasaki K, Yamasaki T, Tateno H Sci Rep. 2018 May 17;8(1):7740. doi: 10.1038/s41598-018-25630-2. PMID:29773815[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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