Computational targeting of allosteric site of MEK1 by quinoline‐based molecules

• Published in: Cell biochemistry and function Vol. 40; no. 5; pp. 481 - 490
• Main Authors: Singh, Rahul, Bhardwaj, Vijay K., Purohit, Rituraj
• Format: Journal Article
• Language: English
• Published: England Wiley Subscription Services, Inc 01.07.2022
• Subjects: allosteric inhibitors; Allosteric properties; Biodegradability; Biodegradation; Breast; Cell proliferation; Clinical trials; Colon; Comparative analysis; Computer applications; Hydrophobicity; Inhibitors; Kinases; Lung cancer; MD simulations; MEK protein; MEK1; MM‐PBSA; Molecular docking; Molecular dynamics; Organic compounds; Phosphorylation; Quinoline; Quinolines; Toxicity; MD simulations; MM-PBSA; MEK1; allosteric inhibitors; quinolines

MEK1 is an attractive target due to its role in selective extracellular‐signal‐regulated kinase phosphorylation, which plays a pivotal role in regulating cell proliferation. Another benefit of targeting the MEK protein is its unique hydrophobic pocket that can accommodate highly selective allosteric...