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1BRV

SOLUTION NMR STRUCTURE OF THE IMMUNODOMINANT REGION OF PROTEIN G OF BOVINE RESPIRATORY SYNCYTIAL VIRUS, 48 STRUCTURES

Summary for 1BRV
Entry DOI10.2210/pdb1brv/pdb
NMR InformationBMRB: 4020
DescriptorPROTEIN G (1 entity in total)
Functional Keywordsattachment protein g of bovine respiratory syncytial virus, immunoglobulin-binding protein, transmembrane, glycoprotein
Biological sourceBovine respiratory syncytial virus (strain 391-2)
Cellular locationVirion membrane. Isoform Secreted glycoprotein G: Secreted: P22261
Total number of polymer chains1
Total formula weight3605.00
Authors
Doreleijers, J.F.,Langedijk, J.P.M.,Hard, K.,Rullmann, J.A.C.,Boelens, R.,Schaaper, W.M.,Van Oirschot, J.T.,Kaptein, R. (deposition date: 1996-03-29, release date: 1997-06-05, Last modification date: 2024-11-06)
Primary citationDoreleijers, J.F.,Langedijk, J.P.,Hard, K.,Boelens, R.,Rullmann, J.A.,Schaaper, W.M.,van Oirschot, J.T.,Kaptein, R.
Solution structure of the immunodominant region of protein G of bovine respiratory syncytial virus.
Biochemistry, 35:14684-14688, 1996
Cited by
PubMed Abstract: 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.
PubMed: 8942628
DOI: 10.1021/bi9621627
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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