3VTT

High Resolution crystal structure of Dengue 3 Envelope protein domain III (ED3)

Summary for 3VTT

• Entry DOI: 10.2210/pdb3vtt/pdb
• Descriptor: Envelope protein E, SULFATE ION (3 entities in total)
• Functional Keywords: immunoglobin like domain, epitope presentation, cellular attachment, viral protein, structural protein
• Biological source: Dengue virus type 3 (DENV-3)
• Cellular location: Capsid protein C: Virion (Potential). Peptide pr: Secreted (By similarity). Small envelope protein M: Virion membrane; Multi-pass membrane protein (By similarity). Envelope protein E: Virion membrane; Multi- pass membrane protein (By similarity). Non-structural protein 1: Secreted. Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Non-structural protein 4A: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P27915
• Total number of polymer chains: 2
• Total formula weight: 23438.70

Authors

Elahi, M.,Islam, M.M.,Kuroda, Y. (deposition date: 2012-06-07, release date: 2012-12-26, Last modification date: 2024-10-30)

Primary citation

Elahi, M.,Islam, M.M.,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, 81:1090-1095, 2013

PubMed 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.

PubMed: 23239402
DOI: 10.1002/prot.24237

Experimental method

X-RAY DIFFRACTION (1.7 Å)