@article{3a0b86f5005a4f2e937c1aa5dbb59ec9,
title = "Solution structure of the envelope protein domain III of dengue-4 virus",
abstract = "The disease dengue (DEN) is caused by four serologically related viruses termed DEN1, DEN2, DEN3 and DEN4. The structure of the ectodomain of the envelope protein has been determined previously for DEN2 and DEN3 viruses. Using NMR spectroscopic methods, we solved the solution structure of domain III (ED3), the receptor-binding domain, of the envelope protein of DEN4 virus, human strain 703-4. The structure shows that the nine amino acid changes in ED3 that separate the sylvatic and human DEN4 strains are surface exposed. Important structural differences between DEN4-rED3 and ED3 domains of DEN2, DEN3 and other flaviviruses are discussed.",
keywords = "Dengue, Dengue-4 virus, Envelope protein domain III, Flavivirus, Nuclear magnetic resonance, Structure",
author = "Volk, \{David E.\} and Lee, \{Yi Chien\} and Xin Li and Varatharasa Thiviyanathan and Gromowski, \{Gregory D.\} and Li Li and Lamb, \{Ashley R.\} and Beasley, \{David W.C.\} and Barrett, \{Alan D.T.\} and Gorenstein, \{David G.\}",
note = "Funding Information: This work was supported by grants U90CCU618754 from the Centers for Disease Control, a grant from the Pediatric Dengue Vaccine Initiative, U01 AI054827 from NIAID, H1296 from the Welch Foundation, P42296LS0000 from the Defense Advanced Research Projects Agency, DAAD17-01-D-0001 from the Defense Threat Reduction Agency, 004952-0038-2003 from the State of Texas Advanced Technology Program, fellowships from the James W. McLaughlin Fellowship Fund to D.W.C.B., and T32 AI 07526 to G.D.G. ",
year = "2007",
month = jul,
day = "20",
doi = "10.1016/j.virol.2007.02.023",
language = "English (US)",
volume = "364",
pages = "147--154",
journal = "Virology",
issn = "0042-6822",
publisher = "Academic Press Inc.",
number = "1",
}