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Lipopolysaccharide recognition by human surfactant protein D (2021)
Presentation / Conference Contribution
Neale, W., Madsen, J., Clark, H., Shrive, A., & Greenhough, T. (2021, August). Lipopolysaccharide recognition by human surfactant protein D. Poster presented at XXV IUCr Congress, Prague, Czech Republic

Bacterial lipopolysaccharide recognition by surfactant protein D (2021)
Presentation / Conference Contribution
Shrive, & Greenhough. (2021, August). Bacterial lipopolysaccharide recognition by surfactant protein D. Presented at XXV IUCr Congress, Prague, Czech Republic

Human surfactant protein D is a collectin and member of the C-type lectin superfamily of proteins that forms an essential part of the mammalian innate immune system. The collectins have been recognised to not only bind to invading pathogens, allowing... Read More about Bacterial lipopolysaccharide recognition by surfactant protein D.

Atomic-resolution crystal structures of the immune protein conglutinin from cow reveal specific interactions of its binding site with N-acetylglucosamine. (2019)
Journal Article
Paterson, J. M., Shaw, A. J., Burns, I., Dodds, A. W., Prasad, A., Reid, K. B., Greenhough, T. J., & Shrive, A. K. (2019). Atomic-resolution crystal structures of the immune protein conglutinin from cow reveal specific interactions of its binding site with N-acetylglucosamine. Journal of biological chemistry, 294(45), 17155-17165. https://doi.org/10.1074/jbc.RA119.010271

Bovine conglutinin is an immune protein that is involved in host resistance to microbes and parasites and interacts with complement component iC3b, agglutinates erythrocytes, and neutralizes influenza A virus. Here, we determined the high-resolution... Read More about Atomic-resolution crystal structures of the immune protein conglutinin from cow reveal specific interactions of its binding site with N-acetylglucosamine..