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Journal Article

A pre-structured helix in the intrinsically disordered 4EBP1.

MPS-Authors
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Sabo,  T. M.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Lee,  D.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

2111547.pdf
(Publisher version), 2MB

Supplementary Material (public)

2111547-Suppl.pdf
(Supplementary material), 2MB

Citation

Kim, D. H., Lee, C., Cho, Y. J., Lee, S. H., Cha, E. J., Lim, J. E., et al. (2015). A pre-structured helix in the intrinsically disordered 4EBP1. Molecular BioSystems, 11(2), 366-369. doi:10.1039/C4MB00532E.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0025-6CEE-1
Abstract
The eIF4E-binding protein 1 (4EBP1) has long been known to be completely unstructured without any secondary structures, which contributed significantly to the proposal of the induced fit mechanism for target binding of intrinsically disordered proteins. We show here that 4EBP1 is not completely unstructured, but contains a pre-structured helix.