A study on the effect of synthetic α-to-β3-amino acid mutations on the binding of phosphopeptides to 14-3-3 proteins

Sebastian A Andrei, Vito Thijssen, Luc Brunsveld, Christian Ottmann, Lech-Gustav Milroy

Onderzoeksoutput: Bijdrage aan tijdschriftTijdschriftartikelAcademicpeer review

6 Citaten (Scopus)
59 Downloads (Pure)

Samenvatting

Here we describe the synthesis of a series of α,β-phosphopeptides, based on the phosphoepitope site on YAP1 (yes-associated protein 1), and the biochemical, biophysical and structural characterization of their binding to 14-3-3 proteins. The impact of systematic mono- and di-substitution of α → β3 amino acid residues around the phosphoserine residue are discussed. Our results confirm the important role played by the +2 proline residue in the thermodynamics and structure of the phosphoepitope/14-3-3 interaction.

Originele taal-2Engels
Pagina's (van-tot)14809-14812
Aantal pagina's4
TijdschriftChemical Communications, ChemComm
Volume55
Nummer van het tijdschrift98
DOI's
StatusGepubliceerd - 5 dec. 2019

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