Figure_3.tif (1.25 MB)
Predicted protein conformational changes.
figure
posted on 2013-02-19, 19:39 authored by Jeffrey R. Kugelman, Michael S. Lee, Cynthia A. Rossi, Sarah E. McCarthy, Sheli R. Radoshitzky, John M. Dye, Lisa E. Hensley, Anna Honko, Jens H. Kuhn, Peter B. Jahrling, Travis K. Warren, Chris A. Whitehouse, Sina Bavari, Gustavo PalaciosLocations of the observed mutations within the structures of EBOV proteins: a) GP truncations – occur right after a disordered region in the crystal structure. The truncation also removes the ends of the trimer (in red). b) GP1,2 – residue E47 (vdW spheres) is near the top of the trimer and, in the X-ray crystal structure (3CSY), makes no interactions with other side chains. c) VP24 – residue K163 forms a tight salt-bridge with D104 on another helix near an undetermined loop in the X-ray structure.
