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High resolution crystal structure of dengue-3 envelope protein domain III suggests possible molecular mechanisms for serospecific antibody recognition.

Authors
  • Elahi, Montasir1
  • Islam, Monirul M
  • Noguchi, Keiichi
  • Yohda, Masafumi
  • Kuroda, Yutaka
  • 1 Department of Biotechnology and Life Science, Graduate School of Engineering, Tokyo University of Agriculture and Technology, Koganei-shi, Tokyo, Japan. , (Japan)
Type
Published Article
Journal
Proteins Structure Function and Bioinformatics
Publisher
Wiley (John Wiley & Sons)
Publication Date
Jun 01, 2013
Volume
81
Issue
6
Pages
1090–1095
Identifiers
DOI: 10.1002/prot.24237
PMID: 23239402
Source
Medline
License
Unknown

Abstract

Dengue viruses are classified into four serotypes. Here, we report a 1.7 Å crystal structure of a recombinant dengue-3 envelope protein domain III (ED3), which contains most of the putative epitopes. Although the fold was well conserved, we found that a local backbone deformation in the first β-strand, which contains the putative epitope-1, occurred upon domain isolation. Furthermore, a comparison with dengue-2 ED3 indicated a large structural change by as much as 4.0 Å at Asp(662), located in epitope-2. These minute structural and surface properties changes observed in the high resolution ED3 structure represent potential determinants for serospecificity and epitope recognition by antibodies.

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