ArticleThe Journal of biological chemistry2012
Near-planar solution structures of mannose-binding lectin oligomers provide insight on activation of lectin pathway of complement.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Towards Metabolic Organic Radical Contrast Agents (mORCAs) for Magnetic Resonance Imaging.Molecules (Basel, Switzerland) · 2025Article
- Collectins and Ficolins.Advances in experimental medicine and biology · 2025Review
- A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin.The Journal of biological chemistry · 2023Article
- The ambiguous role of mannose-binding lectin (MBL) in human immunity.Open medicine (Warsaw, Poland) · 2021Review
- The collagen receptor uPARAP/Endo180 regulates collectins through unique structural elements in its FNII domain.The Journal of biological chemistry · 2020Article
- Exploitation of glycosylation in enveloped virus pathobiology.Biochimica et biophysica acta. General subjects · 2019Review
- Ultrastructure of Highly Ordered Granules in Alveolar Type II Cells in Several Species.Anatomical record (Hoboken, N.J. : 2007) · 2018Article
- Flexibility in Mannan-Binding Lectin-Associated Serine Proteases-1 and -2 Provides Insight on Lectin Pathway Activation.Structure (London, England : 1993) · 2017Article
- Antigliadin Antibodies (AGA IgG) Are Related to Neurochemistry in Schizophrenia.Frontiers in psychiatry · 2017Article
- Article
- Human lectins and their roles in viral infections.Molecules (Basel, Switzerland) · 2015Review
- Scabies mite inactive serine proteases are potent inhibitors of the human complement lectin pathway.PLoS neglected tropical diseases · 2014Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The complement system is a fundamental component of innate immunity that orchestrates complex immunological and inflammatory processes. Complement comprises over 30 proteins that eliminate invading microorganisms while maintaining host cell integrity. Protein-carbohydrate interactions play critical roles in both the activation and regulation of complement. Mannose-binding lectin (MBL) activates the lectin pathway of complement via the recognition of sugar arrays on pathogenic surfaces. To determine the solution structure of MBL, synchrotron x-ray scattering and analytical ultracentrifugation experiments showed that the carbohydrate-recognition domains in the MBL dimer, trimer, and tetramer are positioned close to each other in near-planar fan-like structures. These data were subjected to constrained modeling fits. A bent structure for the MBL monomer was identified starting from two crystal structures for its carbohydrate-recognition domain and its triple helical region. The MBL monomer structure was used to identify 10-12 near-planar solution structures for each of the MBL dimers, trimers, and tetramers starting from 900 to 6,859 randomized structures for each. These near-planar fan-like solution structures joined at an N-terminal hub clarified how the carbohydrate-recognition domain of MBL binds to pathogenic surfaces. They also provided insight on how MBL presents a structural template for the binding and auto-activation of the MBL-associated serine proteases to initiate the lectin pathway of complement activation.
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Registered trials
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