Solution structure and antibody binding studies of the envelope protein domain III from the New York strain of West Nile virus.

@article{Volk2004SolutionSA,
  title={Solution structure and antibody binding studies of the envelope protein domain III from the New York strain of West Nile virus.},
  author={David E Volk and David W. C. Beasley and Deborah A. Kallick and Michael R. Holbrook and Alan D. T. Barrett and David Gorenstein},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 37},
  pages={
          38755-61
        }
}
The solution structure of domain III from the New York West Nile virus strain 385-99 (WN-rED3) has been determined by NMR methods. The West Nile domain III structure is a beta-barrel structure formed from seven anti-parallel beta-strands in two beta-sheets. One anti-parallel beta-sheet consists of beta-strands beta1 (Phe(299)-Asp(307)), beta2 (Val(313)-Tyr(319)), beta4 (Arg(354)-Leu(355)), and beta5 (Lys(370)-Glu(376)) arranged so that beta2 is flanked on either side by beta1 and beta5. The… CONTINUE READING
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