{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jensen JK"],"funding":["NHLBI NIH HHS"],"pagination":["1844-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2548355"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(10)"],"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 str"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["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."],"pmcid":["PMC2548355"],"funding_grant_id":["HL79430","R01 HL079430"],"pubmed_authors":["Jensen JK","Gettins PG"],"additional_accession":[]},"is_claimable":false,"name":"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.","description":"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 str","dates":{"release":"2008-01-01T00:00:00Z","publication":"2008 Oct","modification":"2025-06-01T01:31:52.159Z","creation":"2019-03-26T22:29:10Z"},"accession":"S-EPMC2548355","cross_references":{"pubmed":["18725454"],"doi":["10.1110/ps.036707.108"]}}