1BRV

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

1BRV の概要

• エントリーDOI: 10.2210/pdb1brv/pdb
• NMR情報: BMRB: 4020
• 分子名称: PROTEIN G (1 entity in total)
• 機能のキーワード: attachment protein g of bovine respiratory syncytial virus, immunoglobulin-binding protein, transmembrane, glycoprotein
• 由来する生物種: Bovine respiratory syncytial virus (strain 391-2)
• 細胞内の位置: Virion membrane. Isoform Secreted glycoprotein G: Secreted: P22261
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3605.00

構造登録者

Doreleijers, J.F.,Langedijk, J.P.M.,Hard, K.,Rullmann, J.A.C.,Boelens, R.,Schaaper, W.M.,Van Oirschot, J.T.,Kaptein, R. (登録日: 1996-03-29, 公開日: 1997-06-05, 最終更新日: 2024-11-06)

主引用文献

Doreleijers, 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

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

実験手法

SOLUTION NMR