Rotation-Activated and Cooperative Zipping Characterize Class I Viral Fusion Protein Dynamics.

ABSTRACT: Class I viral fusion proteins are α-helical proteins that facilitate membrane fusion between viral and host membranes through large conformational transitions. Although prefusion and postfusion crystal structures have been solved for many of these proteins, details about how they transition between these states have remained elusive. This work presents the first, to our knowledge, computational survey of transitions between pre- and postfusion configurations for several class I viral fusion proteins using structure-based models to analyze their dynamics. As suggested by their structural similarities, all proteins share common mechanistic features during their transitions that can be characterized by a diffusive rotational search followed by cooperative N- and C-terminal zipping. Instead of

SUBMITTER: Eddy NR 

PROVIDER: S-EPMC5937144 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature