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| 2023-12-21 08:45:41 | onclick： | Scientists reveal secrets of a cancer-causing protein |
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A three-dimensional diagram of the human protein KRAS (blue) interacting with one of its partners, RAF1 (yellow).Source: Center for Genomic Regulation, Barcelona, Spain
Researchers at the Centre for Genomic Regulation in Barcelona, Spain, and the Wellcome Sanger Institute in the UK have fully identified allosteric control sites found in protein KRAS.These are precisely the targets that have received much attention in drug development, new discoveries or key proteins that could help control cancer.The study, published Monday in Nature, provides the first complete control map of KRAS.
KRAS is present in one in 10 human cancers and is more present in fatal types of pancreatic or lung cancer.It's called the "dead star" protein because it's spherical and lacks a good site for drug targeting.For this reason, KRAS has been considered drug-free since it was first discovered in 1982.
The only effective way to control KRAS is through its allosteric communication system.These are molecular signals that work through remote control lock and key mechanisms.To control the protein, a key (compound or drug) that opens the lock (active site) is required.Proteins may also be affected by secondary locks (allosteric sites) located elsewhere on their surface.When a molecule binds to an allosteric site, it causes a change in protein shape, which changes the protein's activity or ability to bind to other molecules, such as changing the internal structure of its main lock.
The study demonstrates a new method to systematically map allosteric sites across proteins.It's like turning on a light that reveals multiple ways to control proteins.
The researchers mapped allosteric sites using deep mutation scanning techniques.It involves creating more than 26,000 variants of the KRAS protein, changing only one or two building blocks (amino acids) at a time.The team examined how these different KRAS variants bind to six other proteins, including those that are critical to KRAS carcinogenesis.The team then used artificial intelligence software to analyze the data, detect heterogeneity and determine the location of known and new therapeutic targets.
The technique shows that KRAS has stronger allosteric sites than expected.Mutations at these sites inhibited the binding of the protein to all three of its main partners, suggesting that widespread inhibition of KRAS activity is possible.A subset of these sites is particularly interesting because they are located in four different pockets that are easily accessible on the surface of the protein and represent promising targets for future drug development.
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