9-Oct-2026
From a rigid dimer to flexible assemblies: revealing the motion of glycan-building enzymes
National Institutes of Natural SciencesPeer-Reviewed Publication
High-speed atomic force microscopy and solution biophysics reveal a striking spectrum of molecular behavior in glycan-building enzymes, from a rigid dimer to flexible, reversible assemblies. POMGNT2 maintained a rigid dimeric architecture, while LARGE1 showed flexible interdomain motion and concentration-dependent assembly. K4CP displayed dramatic opening and closing movements between its domains. The findings uncover diverse dynamic architectures and suggest how structural rigidity and flexibility contribute to distinct roles in glycan synthesis.
- Journal
- International Journal of Molecular Sciences
- Funder
- JST-CREST, JST FOREST Program, Human Glycome Atlas Project, MEXT/JSPS KAKENHI, ExCELLS Advanced Co-creation Platform, ExCELLS "Golgi Atlas Project", Grant-in-Aid for Outstanding Research Group Support Program, Nagoya City University, Joint Research of the Exploratory Research Center on Life and Living Systems (ExCELLS), MEXT Coalition of Universities for Research Excellence Program (CURE), MEXT Project for promoting public utilization of advanced research infrastructure, AMED (Platform Project for Supporting Drug Discovery and Life Science Research, BINDS)