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Updated: Jun 13, 2026
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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
Published on: October 2, 2017
Crystallization and initial X-ray diffraction analysis of a mannose-binding lectin from champedak.
Mads Gabrielsen1, Puteri Shafinaz Abdul-Rahman, Neil W Isaacs
1Glasgow Biomedical Research Centre, Faculty of Biomedical and Life Sciences, Glasgow G12 8QQ, Scotland. m.gabrielsen@bio.gla.ac.uk
Summary
Mannose-binding lectin from champedak fruit exhibits T cell mitogenicity and binds IgE and IgM. This lectin aids in detecting altered serum protein glycosylation, with its crystal structure determined to 2.0 A resolution.
Area of Science:
- Biochemistry
- Structural Biology
- Immunology
Background:
- Mannose-binding lectin (MBL) from champedak (Artocarpus integer) is a homotetrameric protein.
- Previous studies indicate MBL binds IgE and IgM and acts as a T cell mitogen.
- Champedak MBL has demonstrated utility in identifying aberrant glycosylation patterns in serum proteins.
Purpose of the Study:
- To characterize the structural properties of champedak mannose-binding lectin.
- To provide insights into the molecular basis of its biological activities.
- To facilitate further studies on MBL function and applications.
Main Methods:
- Protein purification and characterization.
- Crystallization of champedak MBL at 293 K.
- X-ray diffraction analysis to determine crystal structure.
Main Results:
- The protein was crystallized in space group P2(1)2(1)2(1).
- Unit-cell parameters were determined as a = 76.89, b = 86.22, c = 95.37 A.
- The crystals diffracted X-rays to a resolution of 2.0 A.
Conclusions:
- The structural data obtained provides a foundation for understanding champedak MBL's interactions.
- This work enables further investigation into MBL's role in immune responses and diagnostics.
- The successful crystallization and diffraction pave the way for detailed structural analysis.
