Photocontrol of Smad2, a Multiphosphorylated Cell-Signaling Protein, through Caging of Activating Phosphoserines

Photocontrol of Smad2, a Multiphosphorylated Cell-Signaling Protein, through Caging of Activating Phosphoserines

Expressed‐protein ligation has been used for the semisynthetic preparation of a Smad2 protein with caged activating phosphoserine residues. Biochemical and cell biological experiments show that the caged protein is activated upon irradiation with UV light (see scheme). This sets the stage for the de...

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Veröffentlicht in:Angewandte Chemie International Edition 2004-11, Vol.43 (43), p.5800-5803
Hauptverfasser: Hahn, Michael E., Muir, Tom W.
Format: Artikel
Sprache:eng
Schlagworte:
Binding Sites
bioorganic chemistry
Hydrogen Bonding
Magnetic Resonance Spectroscopy
Molecular Mimicry
Phosphorylation
Phosphoserine - metabolism
Photochemistry
proteins
semisynthesis
Signal Transduction - physiology
X-Ray Diffraction
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Zusammenfassung:Expressed‐protein ligation has been used for the semisynthetic preparation of a Smad2 protein with caged activating phosphoserine residues. Biochemical and cell biological experiments show that the caged protein is activated upon irradiation with UV light (see scheme). This sets the stage for the detailed kinetic analysis of Smad2 function in living cells.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200461141