The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS.
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ABSTRACT:
SUBMITTER: Gosselin P
PROVIDER: S-EPMC3082885 | biostudies-literature | 2011 Apr
REPOSITORIES: biostudies-literature
Publications
The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS.
Gosselin Pauline P Oulhen Nathalie N Jam Murielle M Ronzca Justyna J Cormier Patrick P Czjzek Mirjam M Cosson Bertrand B
Nucleic acids research 20101222 8
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', cha ...[more]
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