Structural highlights
Publication Abstract from PubMed
Dengue viruses are classified into four serotypes. Here, we report a 1.7 A 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 a local backbone deformation in the first beta-strand that 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 A 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. Proteins 2012. (c) 2012 Wiley Periodicals, Inc.
High resolution crystal structure of dengue-3 envelope protein domain III suggests possible molecular mechanisms for serospecific antibody recognition.,Elahi M, Islam MM, Noguchi K, Yohda M, Kuroda Y Proteins. 2012 Dec 14. doi: 10.1002/prot.24237. PMID:23239402[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Elahi M, Islam MM, Noguchi K, Yohda M, Kuroda Y. High resolution crystal structure of dengue-3 envelope protein domain III suggests possible molecular mechanisms for serospecific antibody recognition. Proteins. 2012 Dec 14. doi: 10.1002/prot.24237. PMID:23239402 doi:10.1002/prot.24237
