Structure and engineering of tandem repeat lectins.
- Notova S Univ. Grenoble Alpes, CNRS, CERMAV, 38000 Grenoble, France.
- Bonnardel F Univ. Grenoble Alpes, CNRS, CERMAV, 38000 Grenoble, France; SIB Swiss Institute of Bioinformatics, CH-1227 Geneva, Switzerland; Computer Science Department, UniGe, CH-1227 Geneva, Switzerland.
- Lisacek F SIB Swiss Institute of Bioinformatics, CH-1227 Geneva, Switzerland; Computer Science Department, UniGe, CH-1227 Geneva, Switzerland; Section of Biology, UniGe, CH-1205 Geneva, Switzerland.
- Varrot A Univ. Grenoble Alpes, CNRS, CERMAV, 38000 Grenoble, France.
- Imberty A Univ. Grenoble Alpes, CNRS, CERMAV, 38000 Grenoble, France. Electronic address: anne.imberty@cermav.cnrs.fr.
- 2019-12-17
Published in:
- Current opinion in structural biology. - 2020
English
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, β-trefoils and β-propellers, demonstrated as the most promising scaffold for engineering novel lectins.
- Language
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- English
- Open access status
- green
- Identifiers
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- DOI 10.1016/j.sbi.2019.11.006
- PMID 31841833
- Persistent URL
- https://sonar.ch/global/documents/43909
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