(1) Bijvoet Center for Biomolecular Research, Utrecht University
(2) Department of Mammalian Virology, Institute for Animal Science and Health
(3) Department of Molecular Recognition, Institute for Animal Science and Health
* Present address: Leiden Institute of Chemistry, Leiden University
The three-dimensional solution structure of the immunodominant central conserved region of the attachment protein G (BRSV-G) of bovine respiratory syncytial virus has been determined by nuclear magnetic resonance (NMR) spectroscopy. The 32-residue peptide has a small rigid core composed of two short helices, connected by a type I' turn, and linked by two disulfide bridges. This unique fold comprising only 19 residues is among the smallest stable tertiary structures identified. A characteristic hydrophobic pocket, lined by conserved residues lies at the surface of the peptide and may play a role in receptor binding. This work provides a structural basis for further peptide vaccine development against the severe diseases associated with the respiratory syncytial viruses both in cattle and man.