Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 62, Issue -, Pages 39-47Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2019.11.006
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Funding
- ANR PIA Glyco@Alps [ANR-15-IDEX-02]
- Alliance Campus Rhodanien Co-funds
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Through their ability to bind complex glycoconjugates, lectins have unique specificity and potential for biomedical and biotechnological applications. In particular, lectins with short repeated peptides forming carbohydrate-binding domains are not only of high interest for understanding protein evolution but can also be used as scaffold for engineering novel receptors. Synthetic glycobiology now provides the tools for engineering the specificity of lectins as well as their structure, multivalency and topologies. This review focuses on the structure and diversity of two families of tandem-repeat lectins, that is, beta-trefoils and beta-propellers, demonstrated as the most promising scaffold for engineering novel lectins.
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