9PAI

CLEAVED SUBSTRATE VARIANT OF PLASMINOGEN ACTIVATOR INHIBITOR-1

Summary for 9PAI

• Entry DOI: 10.2210/pdb9pai/pdb
• Descriptor: PROTEIN (PLASMINOGEN ACTIVATOR INHIBITOR-1) residues 19-364, PROTEIN (PLASMINOGEN ACTIVATOR INHIBITOR-1) residues 365-397 (2 entities in total)
• Functional Keywords: serpin, hydrolase inhibitor
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted : P05121 P05121
• Total number of polymer chains: 2
• Total formula weight: 42863.14

Authors

Aertgeerts, K.,De Bondt, H.L.,De Ranter, C.J.,Declerck, P.J. (deposition date: 1999-03-11, release date: 1999-03-19, Last modification date: 2024-04-03)

Primary citation

Aertgeerts, K.,De Bondt, H.L.,De Ranter, C.J.,Declerck, P.J.
Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1.
Nat.Struct.Biol., 2:891-897, 1995

PubMed Abstract: Plasminogen activator inhibitor-1 (PAI-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 PAI-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 PAI-1 provides insights into the molecular determinants responsible for the transition of the stressed active conformation to the thermostable latent conformation.

PubMed: 7552714
DOI: 10.1038/nsb1095-891

Experimental method

X-RAY DIFFRACTION (2.7 Å)