A ligand-reversible dimerization system for controlling protein-protein interactions
نویسندگان
چکیده
منابع مشابه
A ligand-reversible dimerization system for controlling protein-protein interactions.
Chemically induced dimerization provides a general way to gain control over intracellular processes. Typically, FK506-binding protein (FKBP) domains are fused to a signaling domain of interest, allowing crosslinking to be initiated by addition of a bivalent FKBP ligand. In the course of protein engineering studies on human FKBP, we discovered that a single point mutation in the ligand-binding s...
متن کاملG-protein Coupled Receptor Dimerization
A growing body of evidence suggests that GPCRs exist and function as dimers or higher oligomers. The evidence for GPCR dimerization comes from biochemical, biophysical and functional studies. In addition, researchers have shown the occurrence of heterodimerization between different members of the GPCR family. Two receptors can interact with each other to make a dimer through their extracellular...
متن کاملUPA, a universal protein array system for quantitative detection of protein-protein, protein-DNA, protein-RNA and protein-ligand interactions.
Protein-protein interactions have been widely used to study gene expression pathways and may be considered as a new approach to drug discovery. Here I report the development of a universal protein array (UPA) system that provides a sensitive, quantitative, multi-purpose, effective and easy technology to determine not only specific protein-protein interactions, but also specific interactions of ...
متن کامل[Methods for analysis of protein-protein and protein-ligand interactions].
In order to maintain cellular homeostasis, cellular proteins coexist in complex and variable molecular assemblies. Therefore, understanding of major physiological processes at molecular level is based on analysis of protein-protein interaction networks. Firstly, composition of the molecular assembly has to be qualitatively analyzed. In the next step, quantitative bio-chemical properties of the ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2000
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.100101997