The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS. - Sorbonne Université Access content directly
Journal Articles Nucleic Acids Research Year : 2010

The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS.

Abstract

eIF4E binding protein (4E-BP) inhibits translation of capped mRNA by binding to the initiation factor eIF4E and is known to be mostly or completely unstructured in both free and bound states. Using small angle X-ray scattering (SAXS), we report here the analysis of 4E-BP structure in solution, which reveals that while 4E-BP is intrinsically disordered in the free state, it undergoes a dramatic compaction in the bound state. Our results demonstrate that 4E-BP and eIF4E form a 'fuzzy complex', challenging current visions of eIF4E/4E-BP complex regulation.
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Dates and versions

hal-00559465 , version 1 (25-01-2011)

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Pauline Gosselin, Nathalie Oulhen, Murielle Jam, Justyna Ronzca, Patrick Cormier, et al.. The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS.. Nucleic Acids Research, 2010, http://nar.oxfordjournals.org.gate1.inist.fr/content/early/2010/12/21/nar.gkq1306.full. ⟨10.1093/nar/gkq1306⟩. ⟨hal-00559465⟩
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