1Z66

NMR solution structure of domain III of E-protein of tick-borne Langat flavivirus (no RDC restraints)

1Z66 の概要

• エントリーDOI: 10.2210/pdb1z66/pdb
• 関連するPDBエントリー: 1PJW 1S6N 1SVB 1YZO
• NMR情報: BMRB: 5971
• 分子名称: Major envelope protein E (1 entity in total)
• 機能のキーワード: viral protein
• 由来する生物種: Langat virus
• 細胞内の位置: Capsid protein C: Virion (Potential). Peptide pr: Secreted (By similarity). Small envelope protein M: Virion membrane; Multi-pass membrane protein (By similarity). Envelope protein E: Virion membrane; Multi- pass membrane protein (By similarity): P29838
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10612.12

構造登録者

Mukherjee, M.,Dutta, K.,White, M.A.,Cowburn, D.,Fox, R.O. (登録日: 2005-03-21, 公開日: 2006-03-28, 最終更新日: 2024-11-13)

主引用文献

Mukherjee, M.,Dutta, K.,White, M.A.,Cowburn, D.,Fox, R.O.
NMR solution structure and backbone dynamics of domain III of the E protein of tick-borne Langat flavivirus suggests a potential site for molecular recognition.
Protein Sci., 15:1342-1355, 2006

PubMed Abstract: Flaviviruses cause many human diseases, including dengue fever, yellow fever, West Nile viral encephalitis, and hemorrhagic fevers, and are transmitted to their vertebrate hosts by infected mosquitoes and ticks. Domain III of the envelope protein (E-D3) is considered to be the primary viral determinant involved in the virus-host-cell receptor interaction, and thus represents an excellent target for antiviral drug development. Langat (LGT) virus is a naturally attenuated BSL-2 TBE virus and is a model for the pathogenic BSL-3 and BSL-4 viruses in the serogroup. We have determined the solution structure of LGT-E-D3 using heteronuclear NMR spectroscopy. The backbone dynamics of LGT-E-D3 have been investigated using 15N relaxation measurements. A detailed analysis of the solution structure and dynamics of LGT-E-D3 suggests potential residues that could form a surface for molecular recognition, and thereby represent a target site for antiviral therapeutics design.

PubMed: 16731969
DOI: 10.1110/ps.051844006

実験手法

SOLUTION NMR