Title: Mechanisms contributing to the conformational and functional flexibility of plasminogen-activator inhibitor-1
Authors: Aertgeerts, K ×
Debondt, Hl
Deranter, Cj
Declerck, Paul #
Issue Date: Oct-1995
Publisher: Nature publishing co
Series Title: Nature structural biology vol:2 issue:10 pages:891-897
Abstract: Plasminogen activator inhibitor-1 (PAl-1) is unique among the serine proteinase inhibitors (serpins) in that it can adopt at least three different conformations (active, substrate and latent). We report the X-ray structure of a cleaved substrate variant of human PAl-1, which has a new beta-strand s4A formed by insertion of the amino-terminal portion-of the reactive-site loop into beta-sheet A subsequent to cleavage. This is in contrast to the previous suggestion that-the non-inhibitory function of substrate-type serpins is mainly due to an inability of the reactive-site loop to adopt this conformation. Comparison with the structure of latent PAl-1 provides insights into the molecular determinants responsible for the transition of the stressed active conformation to the thermostable latent conformation.
ISSN: 1072-8368
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory for Pharmaceutical Biology (-)
× corresponding author
# (joint) last author

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