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New way of study the conformational changes of the protein dynamic

View:404 Time:2013-03-07

Recently the researchers discovered a new way to study the conformational changes of the protein dynamic, this research  extended by the codon in prokaryotic and eukaryotic tyrosine kinase activity center encoding fluoro-tyrosine, and the conformational change of the research center of the tyrosine kinase activity using 19F nuclear magnetic resonance (NMR), which is based on tyrosylacid kinase activity center conformation provides a powerful tool for screening anticancer drugs.

Tyrosine phosphorylation is an important protein post-translational modification, about this research of study the conformational changes of the protein dynamic, protein plays a crucial role in the enzyme activity, protein conformation and protein interaction adjustment process. The abnormal tyrosine kinase activity center tyrosine phosphorylation is the main reason for the occurrence of many diseases, especially with closely related to the occurrence of tumors. Currently, the design of inhibitors for tyrosine kinase activity center has become the primary means of cancer treatment. However, with the mutation of the tyrosine kinase action of the drug on the loci, more and more patients to existing anticancer drugs produce resistance. Therefore, the development of fast and sensitive method of detecting tyrosine kinase activity center conformation on the design of new anticancer drugs has a very important significance.

This study of the conformational changes of the protein dynamic by the codon extension means to achieve a fluoroalkyl tyrosine active center in the prokaryotic tyrosine kinase Etk Tyr574 locus efficient specific insert, as 19F NMR phosphorylated probe and first Etk active centerinteraction between the pTyr574 with Arg614 direct evidence leading to Etk activation. In addition, the researchers inserted into the fluoroalkyl tyrosine Tyr416 phosphorylation sites in eukaryotic tyrosine kinase c-Src activity center, using 19F NMR detection to dasatinib (for the BCR / Abl and c-Src anticancer drugs) caused by a conformational change in the active center binding and activation status of c-Src. This provides an important means for the study of the mechanism of activation of the tyrosine kinase screening anticancer drugs based tyrosine kinase substrate interactions.

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