Serpins disable their target proteases by formation of an inhibitory complex in which the serpin experiences major structural reordering. How local unfolding allows the serpin to remodel its structure is now mapped by chemical probing. The evolution of functionally important conformationally labile regions has exposed serpins to a risk of aggregation, and indeed many serpinopathy-linked mutations map to the identified labile region.
- Beena Krishnan
- Lila M Gierasch
