Gergely Katona, Professor of Biochemistry at the University of Gothenburg. Credit: Torbjörn Nur Olsson
The structure of less significance
Numerous thousand peptides consisting of 15 amino acids were checked and the scientists had the ability to conclude that it was the amino acid content that affected their binding to survivin, while the structure of the peptides had almost no significance.
” Simple counting things has actually typically been an effective approach in science. Here we counted the variety of amino acids and were able to predict the function of the protein remarkably well,” says Gergely Katona.
The researchers see benefits to this technique of scanning proteins. Device knowing (AI) likewise accelerates the procedure of linking the number and type of amino acids to a certain function. This in turn means that the advancement of new biological drugs can be accelerated.
In the scientists explores this brand-new scanning technique, a completely new function of the protein survivin was likewise found. This protein is mainly prominent in embryo cells and avoids set cell death. In malignant growths, survivin becomes unregulated and therefore assists in the advancement of cancer.
Useful in cancer research
The researchers have now seen that survivin directly affects another protein, PRC2, which switches off and on various functions in the DNA in the cell, like a type of programming. Dysfunctional PRC2 can also be connected to various types of cancer. Todays cancer drugs target both survivin and PRC2, but with the recently found link between survivin and PRC2, the drugs may need to be created in a different way to prevent major side effects.
” We saw that if we reduced the level of survivin, activity in PRC2 increased. The dream for pharmaceutical companies is to find the best targets in the atomic series to be able to stabilize the 2 proteins,” says Gergely Katona.
Referral: “Survivin avoids the polycomb repressor complex 2 from methylating histone 3 lysine 27” by Maja Jensen, Venkataragavan Chandrasekaran, María-José García-Bonete, Shuxiang Li, Atsarina Larasati Anindya, Karin Andersson, Malin C. Erlandsson, Nina Y. Oparina, Björn M. Burmann, Ulrika Brath, Anna R. Panchenko, Maria Bokarewa I. and Gergely Katona, 29 May 2023, iScience.DOI: 10.1016/ j.isci.2023.106976.
The illustration shows how various areas of PRC2 protein (the one on the ideal side) bind to survivin. The color shows binding strength to survivin. Blue suggests the unit in that pixel doesnt bind/binds weakly to survivin, and the intense pink pixels are the strongest binders.
All living cells contain proteins with different functions, depending upon the kind of cell. Scientists have actually discovered a method to identify proteins even without looking at their structure. Their technique is quicker, simpler, and more dependable than previous approaches.
Currently, the general view is that each proteins structure is what controls its function in cells. The atomic sequences, implying how the atoms are organized in the proteins, create the proteins structure and shape. There are many proteins that lack a well-defined structure.
Scientist Gergely Katona at the University of Gothenburg has developed a new method where proteins are scanned based upon the variety of amino acids (or the number of various atoms) they include in order to identify them and their function rather of identifying them based on their structure. With this scanning approach, the scientists had the ability to forecast reasonably reliably which mix of amino acids is needed to bind to the protein survivin. The result was a reliability of about 80 percent, which is much better than when you use the proteins main structures for recognition. The outcomes are now published in the scientific journal iScience.
The illustration shows how different areas of PRC2 protein (the one on the right side) bind to survivin. With this scanning technique, the scientists were able to anticipate reasonably reliably which combination of amino acids is required to bind to the protein survivin. In the researchers experiments with this brand-new scanning method, a totally brand-new function of the protein survivin was likewise discovered. The researchers have now seen that survivin directly influences another protein, PRC2, which changes off and on various functions in the DNA in the cell, like a kind of programming. Todays cancer drugs target both survivin and PRC2, but with the recently discovered link in between survivin and PRC2, the drugs might need to be developed differently to prevent major side effects.
