Artikel

Front Cover: (Chem. Asian J. 7/2024)


<p>Crystal structures of protein kinase complexes with FDA-approved MEK inhibitors showcase the key role of halogen bonds in conferring specificity and affinity for binding halogenated molecules by this important class of biomacromolecules.
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<h2>Abstract</h2>
<p>Kinases are enzymes that play a critical role in governing essential biological processes. Due to their pivotal involvement in cancer cell signaling, they have become key targets in the development of anti-cancer drugs. Among these drugs, those containing the 2,4-dihalophenyl moiety demonstrated significant potential. Here we show how this moiety, particularly the 2-fluoro-4-iodophenyl one, is crucial for the structural stability of the formed drug-enzyme complexes. Crystallographic analysis of reported kinase-inhibitor complex structures highlights the role of the halogen bonding that this moiety forms with specific residues of the kinase binding site. This interaction is not limited to FDA-approved MEK inhibitors, but it is also relevant for other kinase inhibitors, indicating its broad relevance in the design of this class of drugs.</p>

Artikel

Front Cover: (Chem. Asian J. 7/2024)

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Structural Insights on the Role of Halogen Bonding in Protein MEK Kinase‐Inhibitor Complexes

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