Structural Database for Lectins and the UniLectin Web Platform

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Bonnardel, François | Pérez, Serge | Lisacek, Frederique | Imberty, Anne

Edité par CCSD ; Humana Press/Springer Imprint -

International audience. The search for new molecules requires a clear understanding of biosynthesis and degradation pathways. This view applies to most metabolites as well as other molecule types such as glycans whose repertoire is still poorly characterized. Lectins are proteins which recognize specifically and interacts non-covalently with glycans. This particular class of proteins is considered as playing a major role in biology. Glycan-binding is based on multivalence, which gives lectins a unique capacity to interact with surface glycans and significantly contribute to cell-cell recognition and interactions. Lectins have been studied for many years using multiple technologies and part of the resulting information is available online in databases. Unfortunately, the connectivity of these databases with the most popular omics databases (genomics, proteomics and glycomics), remains limited. Moreover, lectin diversity is extended and requires setting out a flexible classification that remains compatible with new sequences and 3D structures that are continuously released. We have designed UniLectin as a new insight in the knowledge of lectins, their classification and their biological role. This platform encompasses UniLectin3D, a curated database of lectin 3D structures that follow a periodically updated classification , a set of comparative and visualizing tools and gradually released modules dedicated to specific lectins predicted in sequence databases. The second module is PropLec, focused on -propeller lectin prediction in all species based on five distinct family profiles. This chapter describes how UniLectin can be used to explore the diversity of lectins, their 3D structures and associated functional information as well as to perform reliable predictions of -propeller lectins.

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