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