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- W2093986989 abstract "Surfactant protein D (SP-D), a C-type lectin, is an important pulmonary host defense molecule. Carbohydrate binding is critical to its host defense properties, but the precise polysaccharide structures recognized by the protein are unknown. SP-D binding to Aspergillus fumigatus is strongly inhibited by a soluble β-(1→6)-linked but not by a soluble β-(1→3)-linked glucosyl homopolysaccharide (pustulan and laminarin, respectively), suggesting that SP-D recognizes only certain polysaccharide configurations, likely through differential binding to nonterminal glucosyl residues. In this study we have computationally docked α/β-d-glucopyranose and α/β-(1→2)-, α/β-(1→3)-, α/β-(1→4)-, and α/β-(1→6)-linked glucosyl trisaccharides into the SP-D carbohydrate recognition domain. As with the mannose-binding proteins, we found significant hydrogen bonding between the protein and the vicinal, equatorial OH groups at the 3 and 4 positions on the sugar ring. Our docking studies predict that α/β-(1→2)-, α-(1→4)-, and α/β-(1→6)-linked but not α/β-(1→3)-linked glucosyl trisaccharides can be bound by their internal glucosyl residues and that binding also occurs through interactions of the protein with the 2- and 3-equatorial OH groups on the glucosyl ring. By using various soluble glucosyl homopolysaccharides as inhibitors of SP-D carbohydrate binding, we confirmed the interactions predicted by our modeling studies. Given the sequence and structural similarity between SP-D and other C-type lectins, many of the predicted interactions should be applicable to this protein family." @default.
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- W2093986989 date "2001-06-08" @default.
- W2093986989 modified "2023-09-25" @default.
- W2093986989 title "Polysaccharide Recognition by Surfactant Protein D: Novel Interactions of a C-Type Lectin with Nonterminal Glucosyl Residues" @default.
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- W2093986989 doi "https://doi.org/10.1021/bi002901q" @default.
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