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Protein Science (2006), 15:1342-1355. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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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

Munia Mukherjee1,3, Kaushik Dutta2,3, Mark A. White1, David Cowburn2 and Robert O. Fox1

1 Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas 77555-0647, USA
2 New York Structural Biology Center, New York, New York 10027, USA

(RECEIVED September 13, 2005; FINAL REVISION February 24, 2006; ACCEPTED February 27, 2006)

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.

Keywords: flavivirus; Langat virus; E protein; E protein domain III; NMR spectroscopy; NMR relaxation; backbone dynamics; residual dipolar coupling; protein conformation; protein–protein interactions


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