Crystallization of Galectin-8 Linker Reveals Intricate Relationship between the N-terminal Tail and the Linker
AbstractGalectin-8 (Gal-8) plays a significant role in normal immunological function as well as in cancer. This lectin contains two carbohydrate recognition domains (CRD) connected by a peptide linker. The N-terminal CRD determines ligand binding specificity, whereas the linker has been proposed to regulate overall Gal-8 function, including multimerization and biological activity. Here, we crystallized the Gal-8 N-terminal CRD with the peptide linker using a crystallization condition that contains Ni2+. The Ni2+ ion was found to be complexed between two CRDs via crystal packing contacts. The coordination between Ni2+ and Asp25 plays an indirect role in determining the structure of β-strand F0 and in influencing the linker conformation which could not be defined due to its dynamic nature. The linker was also shortened in situ and crystallized under a different condition, leading to a higher resolution structure refined to 1.08 Å. This crystal structure allowed definition of a short portion of the linker interacting with the Gal-8 N-terminal tail via ionic interactions and hydrogen bonds. Observation of two Gal-8 N-terminal CRD structures implies that the N-terminal tail and the linker may influence each other’s conformation. In addition, under specific crystallization conditions, glycerol could replace lactose and was observed at the carbohydrate binding site. However, glycerol did not show inhibition activity in hemagglutination assay. View Full-Text
Scifeed alert for new publicationsNever miss any articles matching your research from any publisher
- Get alerts for new papers matching your research
- Find out the new papers from selected authors
- Updated daily for 49'000+ journals and 6000+ publishers
- Define your Scifeed now
Si, Y.; Wang, Y.; Gao, J.; Song, C.; Feng, S.; Zhou, Y.; Tai, G.; Su, J. Crystallization of Galectin-8 Linker Reveals Intricate Relationship between the N-terminal Tail and the Linker. Int. J. Mol. Sci. 2016, 17, 2088.
Si Y, Wang Y, Gao J, Song C, Feng S, Zhou Y, Tai G, Su J. Crystallization of Galectin-8 Linker Reveals Intricate Relationship between the N-terminal Tail and the Linker. International Journal of Molecular Sciences. 2016; 17(12):2088.Chicago/Turabian Style
Si, Yunlong; Wang, Yue; Gao, Jin; Song, Chenyang; Feng, Shiqiong; Zhou, Yifa; Tai, Guihua; Su, Jiyong. 2016. "Crystallization of Galectin-8 Linker Reveals Intricate Relationship between the N-terminal Tail and the Linker." Int. J. Mol. Sci. 17, no. 12: 2088.
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.