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Complex carbohydrate recognition by proteins: Fundamental insights from bacteriophage cell adhesion systems

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Kang,  Yu
Mark Santer, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Santer,  Mark
Mark Santer, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Citation

Broeker, N. K., Andres, D., Kang, Y., Gohlke, U., Schmidt, A., Kunstmann, S., et al. (2016). Complex carbohydrate recognition by proteins: Fundamental insights from bacteriophage cell adhesion systems. Perspectives in Science. doi:10.1016/j.pisc.2016.10.001.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-BE83-8
Abstract
Protein–glycan interactions are ubiquitous in nature. Molecular description of complex formation and the underlying thermodynamics, however, are not well understood due to the lack of model systems. Bacteriophage tailspike proteins (TSP) possess binding sites for bacterial cell surfaces oligosaccharides. In this article we describe the analysis of TSP-oligosaccharide complexes. TSP provide large glycan interaction sites where affinity and specificity are guided by the protein surface solvation and the conformational space sampled by the respective glycan. Furthermore, we describe a computational approach to analyze the conformational space sampled by flexible glycans of bacterial origin, a prerequisite for a thorough understanding of TSP-oligosaccharide interactions.