1brv
SOLUTION NMR STRUCTURE OF THE IMMUNODOMINANT REGION OF PROTEIN G OF BOVINE RESPIRATORY SYNCYTIAL VIRUS, 48 STRUCTURES
OverviewOverview
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. In the 32-residue peptide studied, 19 residues form a small rigid 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 structures known and could therefore serve as an ideal building block for the design of de novo proteins and as a test case for modeling studies. 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 in both cattle and man.
About this StructureAbout this Structure
1BRV is a Single protein structure of sequence from Bovine respiratory syncytial virus. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of the immunodominant region of protein G of bovine respiratory syncytial virus., Doreleijers JF, Langedijk JP, Hard K, Boelens R, Rullmann JA, Schaaper WM, van Oirschot JT, Kaptein R, Biochemistry. 1996 Nov 26;35(47):14684-8. PMID:8942628 Page seeded by OCA on Fri May 2 11:52:49 2008
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- Bovine respiratory syncytial virus
- Single protein
- Boelens, R.
- Doreleijers, J F.
- Hard, K.
- Kaptein, R.
- Langedijk, J P.M.
- Oirschot, J T.Van.
- Rullmann, J A.C.
- Schaaper, W M.
- Attachment protein g of bovine respiratory syncytial virus
- Glycoprotein
- Immunoglobulin-binding protein
- Transmembrane