Phosphate Transfer in Activated Protein Complexes Reveals Interaction Sites. Issue 44 (27th September 2017)

• Record Type: Journal Article
• Authors: Tamara, Sem; Scheltema, Richard A.; Heck, Albert J. R.; Leney, Aneika C.
• Is Part Of: Angewandte Chemie international edition. Volume 56:Issue 44(2017)
• Page Start: 13641
• Page End: 13644
• Publication Date: 2017-09-27
• Subjects: native MS -- phosphorylation -- Pin1 -- protein–protein interactions -- proteomics; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201706749
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: For many proteins, phosphorylation regulates their interaction with other biomolecules. Herein, we describe an unexpected phenomenon whereby phosphate groups are transferred non‐enzymatically from one interaction partner to the other within a binding interface upon activation in the gas phase. Providing that a high affinity exists between the donor and acceptor sites, this phosphate transfer is very efficient and the phosphate groups only ligate to sites in proximity to the binding region. Consequently, such phosphate‐transfer reactions may define with high precision the binding site between a phosphoprotein and its binding partner, as well as reveal that the binding site in this system is retained in the phase transfer from solution to the gas phase. Abstract : Pass the P : Phosphate groups can be transferred non‐enzymatically from one interaction partner to the other during gas‐phase activation. In high‐affinity complexes, this phosphate transfer occurs within the binding site, thereby revealing the interaction interface within the protein/phosphopeptide complex.