Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs
(2023)
Journal Article
Williams, H. M., Moeller, J. B., Burns, I., Schlosser, A., Sorensen, G. L., Greenhough, T. J., Holmskov, U., & Shrive, A. K. (2023). Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs. Journal of Biological Chemistry, 105552. https://doi.org/10.1016/j.jbc.2023.105552
Fibrinogen C-domain containing-1 (FIBCD1) is an immune protein proposed to be involved in host recognition of chitin on the surface of pathogens. As FIBCD1 readily binds to acetylated molecules, we have determined the high-resolution crystal structur... Read More about Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs.