Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization.

ABSTRACT: The serpins (serine proteinase inhibitors) are structurally similar but functionally diverse proteins that fold into a conserved structure and employ a unique suicide substrate-like inhibitory mechanism. Serpins play absolutely critical role in the control of proteases involved in the inflammatory, complement, coagulation and fibrinolytic pathways and are associated with many conformational diseases. Serpin's native state is a metastable state which transforms to a more stable state during its inhibitory mechanism. Serpin in the native form is in the stressed (S) conformation that undergoes a transition to a relaxed (R) conformation for the protease inhibition. During this transition the region called as reactive center loop which interacts with target proteases, inserts itself into the ce

SUBMITTER: Khan MS 

PROVIDER: S-EPMC3268027 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature