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From lectin structure to functional glycomics: principles of the sugar code
Hans-Joachim Gabius1, Sabine André, Jesús Jiménez-Barbero
1Institute of Physiological Chemistry, Ludwig-Maximilians-University Munich, München, Germany. gabius@tiph.vetmed.uni-muenchen.de
Trends in Biochemical Sciences
|April 5, 2011
Summary
Lectins are proteins that bind carbohydrates. Understanding their specificity for cellular glycans is key to the
Area of Science:
- Biochemistry
- Glycobiology
- Molecular Biology
Background:
- Lectins are carbohydrate-binding proteins distinct from antibodies and sensor/transport proteins.
- The 'sugar code' framework highlights the functional importance of lectin-glycan interactions.
- Lectins exhibit diverse structures, including over a dozen folds and varied binding site architectures.
Purpose of the Study:
- To explain the exquisite target specificity of endogenous lectins for cellular glycans.
- To systematically dissect lectin-glycan affinity regulation into six distinct levels.
Main Methods:
- Systematic dissection of affinity regulation into six levels.
- Strategic combination of experimental methods to monitor lectin-glycan interplay.
Main Results:
- Identification of six levels of lectin-glycan affinity regulation.
- Demonstration of how diverse lectin structures contribute to sugar-binding capacity.
Conclusions:
- Understanding lectin-glycan interactions is crucial for deciphering the 'sugar code'.
- A multi-method experimental approach is promising for elucidating lectin specificity and affinity regulation.
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