3CVM

High resolution structure of a stable Plasminogen activator inhibitor type-1 in its protease cleaved form

Summary for 3CVM

• Entry DOI: 10.2210/pdb3cvm/pdb
• Related: 9PAI
• Descriptor: Plasminogen activator inhibitor 1 (2 entities in total)
• Functional Keywords: plasminogen activator inhibitor type-1, cleaved serpin, glycoprotein, plasminogen activation, polymorphism, protease inhibitor, secreted, serine protease inhibitor, blood clotting
• Biological source: Homo sapiens (Human)
• Cellular location: Secreted: P05121
• Total number of polymer chains: 2
• Total formula weight: 88555.34

Authors

Jensen, J.K.,Gettins, P.G.W. (deposition date: 2008-04-18, release date: 2008-08-19, Last modification date: 2023-08-30)

Primary citation

Jensen, J.K.,Gettins, P.G.
High-resolution structure of the stable plasminogen activator inhibitor type-1 variant 14-1B in its proteinase-cleaved form: a new tool for detailed interaction studies and modeling.
Protein Sci., 17:1844-1849, 2008

PubMed Abstract: Wild-type plasminogen activator inhibitor type-1 (PAI-1) rapidly converts to the inactive latent state under conditions of physiological pH and temperature. For in vivo studies of active PAI-1 in cell culture and in vivo model systems, the 14-1B PAI-1 mutant (N150H-K154T-Q319L-M354I), with its stabilized active conformation, has thus become the PAI-1 of choice. As a consequence of the increased stability, the only two forms likely to be encountered are the active or the cleaved form, the latter either free or complexed with target proteinase. We hereby report the first structure of the stable 14-1B PAI-1 variant in its reactive center cleaved form, to a resolution of 2.0 A. The >99% complete structure represents the highest resolved structure of free cleaved PAI-1. This high-resolution structure should be of great use for drug target development and for modeling protein-protein interactions such as those of PAI-1 with vitronectin.

PubMed: 18725454
DOI: 10.1110/ps.036707.108

Experimental method

X-RAY DIFFRACTION (2.02 Å)