title: A rigid lanthanide binding tag to aid NMR studies of a 70 kDa homodimeric coat protein of human norovirus.
abstract: Attachment of human noroviruses to histo blood group antigens is thought to be essential for infection of host cells. Molecular details of the attachment process can be studied in vitro using a variety of NMR experiments. The use of protein NMR based experiments requires assignments of backbone NMR signals. Using uniformly (2)H,(15)N-labeled protruding domains (P-dimers) of a prevalent epidemic human norovirus strain (GII.4 Saga) we have studied the potential of α-l-fucose covalently linked to a rigid lanthanide binding tag to aid backbone assignments using the paramagnetic properties of lanthanide ions. The synthesis of tagged α-l-fucose is reported. Notably, the metal chelating unit connects to the carbohydrate via a triazole linker constructed using click chemistry.
authors.affiliation: Institute of Chemistry, Center for Structural and Cell Biology in Medicine (CSCM), University of Luebeck, Ratzeburger Allee 160, 23538 Luebeck, Germany.
authors.forename: Alvaro
authors.initials: A
authors.lastname: Mallagaray
authors.forename: Gema
authors.initials: G
authors.lastname: Domínguez
authors.forename: Thomas
authors.initials: T
authors.lastname: Peters
authors.forename: Javier
authors.initials: J
authors.lastname: Pérez-Castells
mesh_terms: D001789:Blood Group Antigens / Q000737:chemistry; D036022:Capsid Proteins / Q000737:chemistry*; D019281:Dimerization; D005643:Fucose / Q000737:chemistry; D006801:Humans; D028581:Lanthanoid Series Elements / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D029322:Norovirus / Q000737:chemistry*; D011485:Protein Binding
chemical_list: D001789:Blood Group Antigens; D036022:Capsid Proteins; D028581:Lanthanoid Series Elements; D005643:Fucose