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  Indian J Med Microbiol
 

Figure 4: Docking berberine into the ATP binding site of myosin light-chain kinase. (a) The binding mode of berberine to the ATP binding site of myosin light-chain kinase. Berberine forms two hydrogen bonds with Lys173 and Val221. The negatively charged side chains of Asp285 and Glu269 may stabilize the binding of the positively charged berberine via electrostatic attraction. (b) Illustration of interaction between berberine and myosin light-chain kinase. The binding of berberine to the myosin light-chain kinase is driven by the hydrophobic interaction with residues such as Ala171, Met272, Val202, Ile284, Val158, in addition to two hydrogen bonds

Figure 4: Docking berberine into the ATP binding site of myosin light-chain kinase. (a) The binding mode of berberine to the ATP binding site of myosin light-chain kinase. Berberine forms two hydrogen bonds with Lys173 and Val221. The negatively charged side chains of Asp285 and Glu269 may stabilize the binding of the positively charged berberine via electrostatic attraction. (b) Illustration of interaction between berberine and myosin light-chain kinase. The binding of berberine to the myosin light-chain kinase is driven by the hydrophobic interaction with residues such as Ala171, Met272, Val202, Ile284, Val158, in addition to two hydrogen bonds