A Photochemical Switch for Controlling Protein-Protein Interactions

Autor:	Sonia K. Pollitt, Peter G. Schultz
Rok vydání:	1998
Předmět:	chemistry.chemical_classification Chemistry Effector Mutagenesis Signal transducing adaptor protein General Chemistry GTPase Photochemistry Catalysis Protein–protein interaction Amino acid Biochemistry Side chain Signal transduction
Zdroj:	Angewandte Chemie International Edition. 37:2104-2107
ISSN:	1521-3773 1433-7851
DOI:	10.1002/(sici)1521-3773(19980817)37:15<2104::aid-anie2104>3.0.co;2-z
Popis:	Incorporation of an unnatural amino acid containing a photolabile group in the side chain allows specific interactions between two proteins to be prevented. The photocaged ras protein in which Asp 38 has been substituted by its β-nitrobenzyl ester (Nb) is unable to interact with its effector protein p120-GAP (see drawing below) although it has the same intrinsic GTPase activity. After photocleavage of the Nb group, 50% of the p120-GAP-dependent GTPase activity relative to the wild-type protein is restored.
Databáze:	OpenAIRE
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