2XFB
CHIKUNGUNYA E1 E2 ENVELOPE GLYCOPROTEINS FITTED IN SINDBIS VIRUS cryo- EM MAP
Summary for 2XFB
| Entry DOI | 10.2210/pdb2xfb/pdb |
| Related | 2XFC 3N40 3N42 3N43 3N44 |
| EMDB information | 1121 |
| Descriptor | E1 ENVELOPE GLYCOPROTEIN, E2 ENVELOPE GLYCOPROTEIN (2 entities in total) |
| Functional Keywords | alphavirus, receptor binding, virus, membrane fusion, icosahedral enveloped virus |
| Biological source | CHIKUNGUNYA VIRUS More |
| Total number of polymer chains | 8 |
| Total formula weight | 320702.97 |
| Authors | Voss, J.E.,Vaney, M.C.,Duquerroy, S.,Rey, F.A. (deposition date: 2010-05-21, release date: 2010-11-24, Last modification date: 2024-10-09) |
| Primary citation | Voss, J.E.,Vaney, M.C.,Duquerroy, S.,Vonrhein, C.,Girard-Blanc, C.,Crublet, E.,Thompson, A.,Bricogne, G.,Rey, F.A. Glycoprotein Organization of Chikungunya Virus Particles Revealed by X-Ray Crystallography Nature, 468:709-, 2010 Cited by PubMed Abstract: Chikungunya virus (CHIKV) is an emerging mosquito-borne alphavirus that has caused widespread outbreaks of debilitating human disease in the past five years. CHIKV invasion of susceptible cells is mediated by two viral glycoproteins, E1 and E2, which carry the main antigenic determinants and form an icosahedral shell at the virion surface. Glycoprotein E2, derived from furin cleavage of the p62 precursor into E3 and E2, is responsible for receptor binding, and E1 for membrane fusion. In the context of a concerted multidisciplinary effort to understand the biology of CHIKV, here we report the crystal structures of the precursor p62-E1 heterodimer and of the mature E3-E2-E1 glycoprotein complexes. The resulting atomic models allow the synthesis of a wealth of genetic, biochemical, immunological and electron microscopy data accumulated over the years on alphaviruses in general. This combination yields a detailed picture of the functional architecture of the 25 MDa alphavirus surface glycoprotein shell. Together with the accompanying report on the structure of the Sindbis virus E2-E1 heterodimer at acidic pH (ref. 3), this work also provides new insight into the acid-triggered conformational change on the virus particle and its inbuilt inhibition mechanism in the immature complex. PubMed: 21124458DOI: 10.1038/NATURE09555 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (9 Å) |
Structure validation
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