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Updated: Jul 13, 2026
10:07
Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Subunit assembly of plant lectins
Sharmistha Sinha1, Garima Gupta, Mamannamana Vijayan
1Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India. sinhas@mbu.iisc.ernet.in
Current Opinion in Structural Biology
|August 22, 2007
Summary
Lectins are diverse carbohydrate-binding proteins with similar structures but varied quaternary arrangements. This structural variation creates multivalency, enhancing sugar recognition and biological roles.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Biology
Background:
- Lectins are proteins that recognize and bind carbohydrates.
- They are involved in numerous biological processes.
- Lectins display significant structural diversity.
Purpose of the Study:
- To explore the relationship between lectin structure and function.
- To understand how structural variations contribute to diverse biological roles.
- To investigate the generation of multivalency in lectins.
Main Methods:
- Comparative structural analysis of diverse lectins.
- Examination of secondary, tertiary, and quaternary structures.
- Analysis of carbohydrate-binding specificities and surface topology.
Main Results:
- Lectins exhibit modest variation in secondary and tertiary structures despite diverse specificities.
- Similar tertiary folds can adopt various quaternary structures through subunit reorientation.
- Quaternary structure variations lead to multivalency in sugar recognition and surface topology.
Conclusions:
- Lectin quaternary structure is a key determinant of their functional diversity.
- Variations in subunit arrangement generate multivalency, crucial for biological recognition events.
- Understanding lectin structural dynamics provides insights into carbohydrate-protein interactions.
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