Ontology highlight
ABSTRACT:
SUBMITTER: Bornholdt ZA
PROVIDER: S-EPMC4138722 | biostudies-literature | 2013 Aug
REPOSITORIES: biostudies-literature
Cell 20130801 4
Proteins, particularly viral proteins, can be multifunctional, but the mechanisms behind multifunctionality are not fully understood. Here, we illustrate through multiple crystal structures, biochemistry, and cellular microscopy that VP40 rearranges into different structures, each with a distinct function required for the ebolavirus life cycle. A butterfly-shaped VP40 dimer traffics to the cellular membrane. Once there, electrostatic interactions trigger rearrangement of the polypeptide into a l ...[more]