In AP Biology class, we learned that an allosteric interaction is when an effector (some other kind of molecule) inhibits or activates an enzyme at its allosteric site. When an allosteric enzyme binds to an effector molecule, a conformational change occurs. The allosteric effects of many mutations that cause diseases, such as cancer drivers, cause them to be pathological. Allosteric sites are very difficult to locate because the rules governing how proteins work at the atomic level are hidden out of sight.
A recent discovery reveals newly discovered “secret doors” that control protein function and which could potentially be targeted in order to improve the conditions of cancer, dementia, and infectious diseases. Proteins play a crucial role in all living organisms by fighting diseases, speeding up reactions, acting as messengers, etc. A protein’s structure is essential to its function, and with one change in its sequence if amino acids could result in devastating consequences to a human’s health.
Researchers have previously found success in targeting active sites, and now, with this new method, allosteric sites are identifiable as well. Several treatments have been designed that target a protein’s active site; however, active sites of different proteins look very similar, causing medications to bind and inhibit many different proteins at once. This leads to potential side effects. In contrast, allosteric drugs are one of the most effective medications available today due to the specificity of allosteric sites. The new method in targeting allosteric sites has been used to chart the first map ever of these allosteric sites in two of the most common human proteins. This new approach may be a game changer for drug discovery, leading to more effective medications, and enabling researchers to locate and exploit vulnerabilities in any protein—even those previously thought to be untreatable!
Please feel free to leave your thoughts or questions in the comments! 🙂
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