2GG1

NMR solution structure of domain III of the E-protein of tick-borne Langat flavivirus (includes RDC restraints)

Replaces:  1YZO

Summary for 2GG1

• Entry DOI: 10.2210/pdb2gg1/pdb
• Related: 1SVB 1Z66
• NMR Information: BMRB: 6800
• Descriptor: Genome polyprotein (1 entity in total)
• Functional Keywords: viral protein, domain iii
• Biological source: Langat virus
• Total number of polymer chains: 1
• Total formula weight: 11176.67

Authors

Mukherjee, M.,Dutta, K.,White, M.A.,Cowburn, D.,Fox, R.O. (deposition date: 2006-03-23, release date: 2006-04-25, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

SOLUTION NMR