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Structural Biology Turned on Its Head
Author(s) -
Bouvignies Guillaume,
Blackledge Martin
Publication year - 2015
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201500101
Subject(s) - eukaryotic translation , phosphorylation , eif4e , folding (dsp implementation) , eukaryotic initiation factor , translation (biology) , initiation factor , biophysics , nuclear magnetic resonance spectroscopy , protein folding , microbiology and biotechnology , biology , computational biology , chemistry , biochemistry , stereochemistry , messenger rna , gene , electrical engineering , engineering
NMR spectroscopy and ITC have recently been combined to demonstrate how phosphorylation of the intrinsically disordered eukaryotic translation initiation factor 4E‐binding protein 2 (4E‐BP2) induces folding into a stable three‐dimensional structure. The classical structure–function paradigm is inverted, with phosphorylation‐induced folding inhibiting binding to the eukaryotic translation initiation factor 4E (eIF4E) and thereby contributing to regulation of the interaction.