SerpinB12 inhibitors target and inhibit the activity of SerpinB12, a member of the serine protease inhibitor (serpin) superfamily. Serpins are known for their role in regulating proteases, enzymes that catalyze the breakdown of proteins. SerpinB12, in particular, is involved in inhibiting specific serine proteases. The structure of SerpinB12, like other serpins, is characterized by a conserved tertiary structure with a reactive center loop (RCL) that acts as a bait for target proteases. Upon interaction with a protease, the RCL undergoes a conformational change, leading to the inhibition of the protease's enzymatic activity. The functionality of SerpinB12 is integral to various physiological processes, including inflammation and coagulation. Inhibitors of SerpinB12 are designed to selectively interact with the protein, aiming to modulate its protease-inhibiting activity by targeting the RCL or other key structural elements essential for its function.
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