Predicted protein conformational changes. R. KugelmanJeffrey LeeMichael S. A. RossiCynthia E. McCarthySarah R. RadoshitzkySheli DyeJohn M. E. HensleyLisa HonkoAnna H. KuhnJens B. JahrlingPeter WarrenTravis K. A. WhitehouseChris BavariSina PalaciosGustavo 2013 <p>Locations 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) GP<sub>1,2</sub> – 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.</p>