2R6P
Fit of E protein and Fab 1A1D-2 into 24 angstrom resolution cryoEM map of Fab complexed with dengue 2 virus.
Summary for 2R6P
| Entry DOI | 10.2210/pdb2r6p/pdb |
| EMDB information | 1418 |
| Descriptor | Major envelope protein E, Heavy chain of 1A1D-2, Light chain of 1A1D-2 (3 entities in total) |
| Functional Keywords | fab, dengue, virus, neutralization, virus-immune system complex, icosahedral virus, virus/immune system |
| Biological source | Dengue virus 2 Puerto Rico/PR159-S1/1969 More |
| Total number of polymer chains | 7 |
| Total formula weight | 221965.94 |
| Authors | Lok, S.M.,Kostyuchenko, V.K.,Holdaway, H.A.,Chipman, P.R.,Kuhn, R.J.,Rossmann, M.G. (deposition date: 2007-09-06, release date: 2007-12-25, Last modification date: 2024-02-21) |
| Primary citation | Lok, S.M.,Kostyuchenko, V.,Nybakken, G.E.,Holdaway, H.A.,Battisti, A.J.,Sukupolvi-Petty, S.,Sedlak, D.,Fremont, D.H.,Chipman, P.R.,Roehrig, J.T.,Diamond, M.S.,Kuhn, R.J.,Rossmann, M.G. Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins. Nat.Struct.Mol.Biol., 15:312-317, 2008 Cited by PubMed Abstract: The monoclonal antibody 1A1D-2 has been shown to strongly neutralize dengue virus serotypes 1, 2 and 3, primarily by inhibiting attachment to host cells. A crystal structure of its antigen binding fragment (Fab) complexed with domain III of the viral envelope glycoprotein, E, showed that the epitope would be partially occluded in the known structure of the mature dengue virus. Nevertheless, antibody could bind to the virus at 37 degrees C, suggesting that the virus is in dynamic motion making hidden epitopes briefly available. A cryo-electron microscope image reconstruction of the virus:Fab complex showed large changes in the organization of the E protein that exposed the epitopes on two of the three E molecules in each of the 60 icosahedral asymmetric units of the virus. The changes in the structure of the viral surface are presumably responsible for inhibiting attachment to cells. PubMed: 18264114DOI: 10.1038/nsmb.1382 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (24 Å) |
Structure validation
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