In:
Angewandte Chemie, Wiley, Vol. 128, No. 25 ( 2016-06-13), p. 7292-7295
Abstract:
Lack of regulation of the interaction between the eIF4E/eIF4G subunits of the translation initiation factor complex eIF4F is a hallmark of cancer. The inhibitor 4EGI‐1 binds to eIF4E, thereby preventing association with eIF4G through an allosteric mechanism. NMR spectroscopy and MD simulations were used to obtain a mechanistic description of the role of correlated dynamics in this allosteric regulation. We show that binding of 4EGI‐1 perturbs native correlated motions and increases correlated fluctuations in part of the eIF4G binding site.
Type of Medium:
Online Resource
ISSN:
0044-8249
,
1521-3757
DOI:
10.1002/ange.v128.25
DOI:
10.1002/ange.201603254
Language:
English
Publisher:
Wiley
Publication Date:
2016
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514305-6
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505872-7
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1479266-7
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506259-7
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