MSK1 Inhibitors

H-89 dihydrochloride is a selective inhibitor of MSK1, a kinase involved in the regulation of various signaling pathways. Its unique structure allows for specific interactions with the ATP-binding site of MSK1, effectively blocking phosphorylation events. This inhibition alters downstream signaling cascades, particularly those related to gene expression and cellular response to stress. The compound's hydrophilic nature enhances solubility, facilitating its interaction with target proteins in aqueous environments.

KT 5720 is a selective inhibitor of MSK1, characterized by its ability to disrupt the kinase's activity through competitive binding at the ATP site. This compound exhibits unique molecular interactions that stabilize the inactive conformation of MSK1, thereby preventing substrate phosphorylation. Its distinct hydrophobic regions contribute to its binding affinity, influencing reaction kinetics and modulating cellular signaling pathways without affecting other kinases.

Ro 31-8220 is a potent inhibitor of MSK1, known for its unique ability to interfere with the kinase's phosphorylation activity. It selectively binds to the ATP-binding site, altering the enzyme's conformation and effectively blocking substrate access. The compound's specific interactions with key amino acid residues enhance its selectivity, while its structural features promote a favorable binding environment, impacting downstream signaling cascades and cellular responses.

Fasudil, Monohydrochloride Salt, acts as a selective modulator of MSK1 by engaging in unique molecular interactions that stabilize the enzyme's inactive conformation. Its binding affinity is influenced by specific hydrogen bonding and hydrophobic interactions with critical residues, which alters the enzyme's kinetic properties. This compound's distinct structural characteristics facilitate a nuanced regulation of signaling pathways, ultimately affecting cellular dynamics and responses.

Bisindolylmaleimide III, Hydrochloride serves as a potent inhibitor of MSK1, characterized by its ability to disrupt key phosphorylation events. Its unique structure allows for specific interactions with the ATP-binding site, leading to altered enzyme conformation and reduced catalytic activity. The compound's selective binding profile is influenced by steric hindrance and electrostatic interactions, which modulate downstream signaling cascades and cellular responses.

HA-1077 dihydrochloride acts as a selective inhibitor of MSK1, showcasing a unique ability to interfere with the enzyme's phosphorylation mechanisms. Its distinct molecular architecture facilitates targeted interactions with specific residues within the active site, promoting conformational changes that hinder enzymatic function. The compound's reactivity is influenced by its halide groups, which enhance its binding affinity and specificity, ultimately impacting various signaling pathways and cellular dynamics.

CKI-7 dihydrochloride serves as a potent inhibitor of MSK1, characterized by its ability to disrupt kinase activity through unique binding interactions. The compound's structural features allow it to engage selectively with key amino acid residues, altering the enzyme's conformation and inhibiting its phosphorylation activity. Its halide components contribute to enhanced solubility and reactivity, influencing the kinetics of enzyme-substrate interactions and modulating downstream signaling cascades.

A specific inhibitor of MSK1 that can suppress MSK1-mediated gene expression and cellular responses.

A natural compound that has been shown to inhibit MSK1 activity by directly targeting its kinase domain.

A non-selective adenosine receptor antagonist that has been reported to inhibit MSK1 activation.