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., …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.