Conformational plasticity of the VEEV macro domain is important for binding of ADP-ribose.

Garyfallia I Makrynitsa,Dioni Ntonti,Konstantinos D Marousis,Maria Birkou,Minos-Timotheos Matsoukas,Sam Asami,Detlef Bentrop,Nicolas Papageorgiou,Bruno Canard,Bruno Coutard,Georgios A Spyroulias

Journal of Structural Biology（2019）

引用 14|浏览56

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摘要

•ADPr’s binding triggers conformational changes to the whole VEEV macro domain.•High flexibility of the loops β5-α3 and α3-β6 assist the ADPr’s binding.•Loops around ADPr site undergo a transition pathway between apo and complex state.

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关键词

Viral macro domain,ADP-ribose,Conformational dynamics,NMR spectroscopy,15N relaxation,Normal mode analysis

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