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.

SUBMITTER: Gosselin P 

PROVIDER: S-EPMC3082885 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature