Journal of Molecular Biology, 438, 5, 2026, 169638
DOI: https://doi.org/10.1016/j.jmb.2026.169638
The Galectin protein family consists of proteins that interact with glycolipid and glycoprotein containing membranes to regulate many cellular and immune functions. Each Galectin is composed of two carbohydrate binding domains, but the exact carbohydrates bound by these domains differs between Galectins. The Vander Zanden group at University of Colorado, Colorado Springs conducted x-ray reflectivity experiments here at ChemMatCARS to determine the orientation of the two carbohydrate binding domains of Galectin-4 and Galectin-8 bound to glycolipid-containing monolayers at the air-water interface. Galectin-4’s domains both interact with the same carbohydrate and the x-ray data resolved both domains directly at the interface. Meanwhile, only one of Galectin-8’s domains bound the monolayer with the other domain extended. This work demonstrates that x-ray reflectivity can be used to characterize the binding conformational dynamics of proteins at the interface.
William R.K. Talley1 †, Daniel Bazan1 †, Jaroslaw Majewski2 3, Herbert Kaltner4, Crystal M. Vander Zanden1*
1Department of Chemistry and Biochemistry, University of Colorado, Colorado Springs, 1420 Austin Bluffs Pkwy, Colorado Springs, CO 80918, USA
2Department of Chemical and Biological Engineering and Center for Biomedical Engineering, University of New Mexico, MSC01 1120, 1 University of New Mexico, Albuquerque, NM 87131, USA
3Department of Chemistry, University of Warsaw, Pasteura Street 1, 02-093 Warsaw, Poland
4Department of Veterinary Sciences, Chair of Biochemistry and Chemistry, Ludwig-Maximilians-Universität, Lena-Christ-Strasse 48, 82152 Martinsried, Planegg, Germany