Related Experiment Video
Updated: Jun 24, 2025

Author Spotlight: Advancing Protein Glycosylation Research Using a Fully Automated System
Published on: June 28, 2024
Tandem-repeat lectins: structural and functional insights
Francisco H Olvera-Lucio1, Héctor Riveros-Rosas2, Adrián Quintero-Martínez1
1Instituto de Química, Universidad Nacional Autónoma de México, Ciudad de México, Coyoacán 04510, Mexico.
Tandem-repeat lectins possess inherent multivalency through intrachain repeats, distinct from oligomerization. This systematic review defines and categorizes these lectins, revealing new insights for biotechnological applications.
Area of Science:
- Biochemistry and Structural Biology
- Glycobiology
- Molecular Evolution
Background:
- Multivalency is crucial for lectin function, influencing glycan cross-linking.
- Lectins achieve multivalency via oligomerization or tandemly repeated carbohydrate recognition domains (CRDs).
- Tandem-repeat lectins possess inherent multivalency, independent of complex oligomerization processes.
Purpose of the Study:
- To establish a unified definition for tandem-repeat lectins.
- To systematically review the folding and phyletic diversity of tandem-repeat lectins.
- To explore the functional and structural characteristics of these lectins.
Main Methods:
- Systematic literature review focusing on tandem-repeat lectins.
- Analysis of folding patterns and phyletic distribution.
- Categorization of lectins based on repeated CRDs and associated functions.
Main Results:
- Proposed definition: multivalent lectins with intrachain tandem CRD repeats, independent of oligomerization.
- Identified nine distinct folding classes for tandem-repeat lectins, linked to specific biological functions.
- Discovered previously undocumented tandem-repeat lectins, expanding knowledge of their diversity.
Conclusions:
- Tandem-repeat lectins represent a distinct class of multivalent proteins with inherent structural advantages.
- The proposed classification provides a framework for understanding their diverse functions and evolutionary origins.
- Further research can leverage these findings for medical and biotechnological advancements, including neolectin design.
Related Concept Videos
Selectins
Peptide Identification Using Tandem Mass Spectrometry
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Ligand Binding and Linkage
Structural Protein Function
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...

