1K4R

Structure of Dengue Virus


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 24.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Starting Model: experimental
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This is version 1.4 of the entry. See complete history


Literature

Structure of dengue virus: implications for flavivirus organization, maturation, and fusion.

Kuhn, R.J.Zhang, W.Rossmann, M.G.Pletnev, S.V.Corver, J.Lenches, E.Jones, C.T.Mukhopadhyay, S.Chipman, P.R.Strauss, E.G.Baker, T.S.Strauss, J.H.

(2002) Cell 108: 717-725

  • DOI: https://doi.org/10.1016/s0092-8674(02)00660-8
  • Primary Citation of Related Structures:  
    1K4R

  • PubMed Abstract: 

    The first structure of a flavivirus has been determined by using a combination of cryoelectron microscopy and fitting of the known structure of glycoprotein E into the electron density map. The virus core, within a lipid bilayer, has a less-ordered structure than the external, icosahedral scaffold of 90 glycoprotein E dimers. The three E monomers per icosahedral asymmetric unit do not have quasiequivalent symmetric environments. Difference maps indicate the location of the small membrane protein M relative to the overlaying scaffold of E dimers. The structure suggests that flaviviruses, and by analogy also alphaviruses, employ a fusion mechanism in which the distal beta barrels of domain II of the glycoprotein E are inserted into the cellular membrane.


  • Organizational Affiliation

    Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA. [email protected]


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MAJOR ENVELOPE PROTEIN E
A, B, C
395Chimeric Tick-borne encephalitis virus/Dengue virus 4Mutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for C3V005 (Chimeric Tick-borne encephalitis virus/Dengue virus 4)
Explore C3V005 
Go to UniProtKB:  C3V005
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupC3V005
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 24.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONOTHER

Structure Validation

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Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2002-03-13
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-07-18
    Changes: Data collection
  • Version 1.4: 2024-10-30
    Changes: Data collection, Database references, Derived calculations, Refinement description, Structure summary