| Abstract
| - The three-dimensional solution structure of the immunodominantcentral conserved region ofthe attachment protein G (BRSV-G) of bovine respiratory syncytial virushas been determined by nuclearmagnetic resonance (NMR) spectroscopy. In the 32-residue peptidestudied, 19 residues form a smallrigid core composed of two short helices, connected by a type I‘ turn,and linked by two disulfide bridges.This unique fold is among the smallest stable tertiary structuresknown and could therefore serve as anideal building block for the design of de novo proteins andas a test case for modeling studies. Acharacteristic hydrophobic pocket, lined by conserved residues, lies atthe surface of the peptide and mayplay a role in receptor binding. This work provides a structuralbasis for further peptide vaccinedevelopment against the severe diseases associated with the respiratorysyncytial viruses in both cattleand man.
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