1. The protease domain of this protein is thought to be cleaved and secreted into cell media after autocleavage.
  2. Activation of the matriptase zymogen requires sequential N-terminal cleavage, activation site autocleavage, and transient association with HAI-1.
  3. The N-terminal prodomain has a flexible crystal structure and is responsible for regulating PCSK9 function by interacting with and blocking the catalytic domain, which otherwise binds the epidermal growth factor-like repeat A ( EGF-A ) domain of the LDLR . While previous studies indicated that the C-terminal domain was uninvolved in binding LDLR, a recent study by Du et al . demonstrated that the C-terminal domain does bind LDLR . The secretion of PCSK9 is largely dependent on the autocleavage of the signal peptide and N-terminal prodomain, though the N-terminal prodomain retains its association with the catalytic domain.


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