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Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family

An Erratum to this article was published on 01 August 1995

Abstract

Tetrameric Galanthus nivalis agglutinin (50,000 Mr) belongs to a super-family of α-D-mannose-specific plant bulb lectins known to be potent inhibitors of retroviruses. The 2.3 Å crystal structure of this lectin complexed with methyl α-D-mannose reveals a novel three-fold symmetric β-sheet polypeptide fold. Three antiparallel four-stranded β-sheets, each with a conserved mannose-binding site, are arranged as a 12-stranded β-barrel. The tetramer displays 222 symmetry. Pairs of monomers form stable dinners through C-terminal strand exchange. The so formed hybrid β-sheets are the sites for high affinity mannose binding in the dimer interface. Occupancy observed at corresponding sites in other β-sheets suggests a potential for twelve sites per tetramer.

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Hester, G., Kaku, H., Goldstein, I. et al. Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family. Nat Struct Mol Biol 2, 472–479 (1995). https://doi.org/10.1038/nsb0695-472

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