Review Article
Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization
Table 3
Unfavourable interactions that contribute to the metastability of the native antitrypsin. Nonideal interactions include the presence of hydrophobic pockets, overpacking of side-chains, the burial of polar groups, cavities in the hydrophobic core of the protein and polar nonpolar interactions [40]. Lys-335 is one of the residues in antitrypsin that has been shown to play a crucial role in conformational switch during the process of inhibition. Local strain due to Lys-335 interactions in the native state is critical for the inhibitory activity.
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