open access

https://hdl.handle.net/2115/45034

The Structure of Physarum polycephalum Hemagglutinin I Suggests a Minimal Carbohydrate Recognition Domain of Legume Lectin Fold

英語

up-and-down β-sheet

2011-01-14

Elsevier

Journal of Molecular Biology

405(2)

560-569

Physarum polycephalum hemagglutinin I is a 104-residue protein that is secreted to extracellular space. The crystal structure of hemagglutinin I has a β-sandwich fold found among lectin structures, such as legume lectins and galectins. Interestingly, the β-sandwich of hemagglutinin I lacks a jelly roll motif and is essentially composed of two simple up-and-down β-sheets. This up-and-down β-sheet motif is well conserved in other lectins derived from animals, plants, bacteria, and viruses. It is more noteworthy that the up-and-down β-sheet motif includes many residues that make contact with the target carbohydrates. Our NMR data demonstrate that hemagglutinin I lacking a jelly roll motif also binds to its target glycopeptide. Taken together, the up-and-down β-sheet motif provides a fundamental scaffold for the binding of legume lectin-like proteins to the target carbohydrates, and the structure of hemagglutinin I suggests a minimal carbohydrate recognition domain.

学術雑誌論文

Accepted Manuscript

0022-2836