Dissecting mechanism of coupled folding and binding of an intrinsically disordered protein by chemical synthesis of conformationally constrained analogues.

Date publication

juin 2017

Journal

Chemical communications (Cambridge, England)

Auteurs

Membres identifiés du Cancéropôle Est :
Dr BIRCK Catherine

Tous les auteurs :
Schmidtgall B, Chaloin O, Bauer V, Sumyk M, Birck C, Torbeev V

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/28604862

Résumé

Non-canonical α-methyl amino acids were incorporated at various sites in the sequence of intrinsically disordered activation domain from the p160 transcriptional co-activator (ACTR) to facilitate the formation of α-helical structures. Kinetic and thermodynamic data confirm the induced fit mechanism of complex formation between the synthesized ACTR variants and the nuclear co-activator binding domain (NCBD).

Mots clés

Amino Acids, chemistry, Intrinsically Disordered Proteins, chemical synthesis, Kinetics, Protein Binding, Protein Conformation, Protein Folding, Thermodynamics, Transcription Factors, chemistry

Référence

Chem. Commun. (Camb.). 2017 Jun 29;53(53):7369-7372