Identification of a PAI-1-binding site within an intrinsically disordered region of vitronectin.

ABSTRACT: The serine protease inhibitor, plasminogen activator inhibitor Type-1 (PAI-1) is a metastable protein that undergoes an unusual transition to an inactive conformation with a short half-life of only 1-2 hr. Circulating PAI-1 is bound to a cofactor vitronectin, which stabilizes PAI-1 by slowing this latency conversion. A well-characterized PAI-1-binding site on vitronectin is located within the somatomedin B (SMB) domain, corresponding to the first 44 residues of the protein. Another PAI-1 recognition site has been identified with an engineered form of vitronectin lacking the SMB domain, yet retaining PAI-1 binding capacity (Schar, Blouse, Minor, Peterson. J Biol Chem. 2008;283:28487-28496). This additional binding site is hypothesized to lie within an intrinsically disordered domain (IDD) o

SUBMITTER: Chu Y 

PROVIDER: S-EPMC6954738 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature