Insights into the homo-oligomerization properties of N-terminal coiled-coil domain of Ebola virus VP35 protein

Insights into the homo-oligomerization properties of N-terminal coiled-coil domain of Ebola virus... •Experimental assessment of the full length EBOV VP35 homo-oligomerization profile.•In silico 3D model prediction of the yet unsolved EBOV VP35 coiled-coil domain.•Structural characterization of self-assembly of di/tri/tetra-mers by MD simulations.•Tetrameric species might originate as multiples of a fundamental dimeric unit.•Biochemical and computational results advance understanding of VP35 oligomerization. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Virus Research Elsevier

Insights into the homo-oligomerization properties of N-terminal coiled-coil domain of Ebola virus VP35 protein

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Publisher
Elsevier
Copyright
Copyright © 2018 Elsevier B.V.
ISSN
0168-1702
D.O.I.
10.1016/j.virusres.2018.02.003
Publisher site
See Article on Publisher Site

Abstract

•Experimental assessment of the full length EBOV VP35 homo-oligomerization profile.•In silico 3D model prediction of the yet unsolved EBOV VP35 coiled-coil domain.•Structural characterization of self-assembly of di/tri/tetra-mers by MD simulations.•Tetrameric species might originate as multiples of a fundamental dimeric unit.•Biochemical and computational results advance understanding of VP35 oligomerization.

Journal

Virus ResearchElsevier

Published: Mar 2, 2018

References

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