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- W1629300521 abstract "This chapter focuses on hevein domains and presents an attractive model to study carbohydrate–protein interactions at atomic resolution. Among the various biological processes in which carbohydrates are involved as biochemical signals, it is noteworthy that many plants harbor defense proteins (lectins) against pathogenic attack. These proteins are able to bind to chitin. This natural biopolymer is a key structural component of the cell wall of fungi and of the exoskeleton of invertebrates such as insects, nematodes, and arthropods. Direct binding to the saccharide can occur for the respective lectin, while a particular domain can also be instrumental for chitin-degrading enzymes. The antifungal activity of plant chitinases is largely restricted to those chitinases that contain a noncatalytic, plant-specific, chitin-binding domain (ChBD), also termed as “hevein domain.” This domain displays a common structural motif of 30–43 residues, rich in glycine and cysteine residues in highly conserved positions and organized around a four-disulfide core. The chapter explains the concepts related to protein–carbohydrate interactions and elaborates the basic techniques for analyzing sugar–hevein interactions. It also discusses the structure of the Hevein–Saccharide complexes." @default.
- W1629300521 created "2016-06-24" @default.
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- W1629300521 date "2006-01-01" @default.
- W1629300521 modified "2023-10-01" @default.
- W1629300521 title "Hevein Domains: An Attractive Model to Study Carbohydrate–Protein Interactions at Atomic Resolution" @default.
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