Structural characterisation of the native fetuin-binding protein Scilla campanulata agglutinin: a novel two-domain lectin |
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Authors: | Wright L M Reynolds C D Rizkallah P J Allen A K Van Damme E J Donovan M J Peumans W J |
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Institution: | School of Biomolecular Sciences, Max Perutz Building, Liverpool John Moores University, Liverpool, UK. |
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Abstract: | The three-dimensional structure of a 244-residue, multivalent, fetuin-binding lectin, SCAfet, isolated from bluebell (Scilla campanulata) bulbs, has been solved at 3.3 A resolution by molecular replacement using the coordinates of the 119-residue, mannose-binding lectin, SCAman, also from bluebell bulbs. Unlike most monocot mannose-binding lectins, such as Galanthus nivalis agglutinin from snowdrop bulbs, which fold into a single domain, SCAfet contains two domains with approximately 55% sequence identity, joined by a linker peptide. Both domains are made up of a 12-stranded beta-prism II fold, with three putative carbohydrate-binding sites, one on each subdomain. SCAfet binds to the complex saccharides of various animal glycoproteins but not to simple sugars. |
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