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 |
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| container_title | Angewandte Chemie International Edition |
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| creator | Hahn, Michael E. Muir, Tom W. |
| description | 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. |
| doi_str_mv | 10.1002/anie.200461141 |
| format | Article |
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| identifier | ISSN: 1433-7851 |
| ispartof | Angewandte Chemie International Edition, 2004-11, Vol.43 (43), p.5800-5803 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Binding Sites bioorganic chemistry Hydrogen Bonding Magnetic Resonance Spectroscopy Molecular Mimicry Phosphorylation Phosphoserine - metabolism Photochemistry proteins semisynthesis Signal Transduction - physiology X-Ray Diffraction |
| title | Photocontrol of Smad2, a Multiphosphorylated Cell-Signaling Protein, through Caging of Activating Phosphoserines |
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