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• W1983256441 abstract "Plasminogen activator inhibitor 1 (PAI-1) is the main inhibitor of plasminogen activators and plays an important role in many pathophysiological processes. Like other members of the serpin family, PAI-1 has a reactive center consisting of a mobile loop (RCL) with P1 and P1' residues acting as a bait for cognate protease. In contrast to the other serpins, PAI-1 loses activity by spontaneous conversion to an inactive latent form. This involves full insertion of the RCL into beta-sheet A. To search for molecular determinants that could be responsible for conversion of PAI-1 to the latent form, we studied the conformation of the RCL in active PAI-1 in solution. Intramolecular distance measurements by donor-donor energy migration and probe quenching methods reveal that the RCL is located much closer to the core of PAI-1 than has been suggested by the recently resolved X-ray structures of stable PAI-1 mutants. Disulfide bonds can be formed in double-cysteine mutants with substitutions at positions P11 or P13 of the RCL and neighboring residues in beta-sheet A. This suggests that the RCL may be preinserted up to residue P13 in active PAI-1, and possibly even to residue P11. We propose that the close proximity of the RCL to the protein core, and the ability of the loop to preinsert into beta-sheet A is a possible reason for PAI-1 being able to convert spontaneously to its latent form." @default.
• W1983256441 created "2016-06-24" @default.
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• W1983256441 date "2004-01-01" @default.
• W1983256441 modified "2023-09-25" @default.
• W1983256441 title "The Reactive-center Loop of Active PAI-1 is Folded Close to the Protein Core and can be Partially Inserted" @default.
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• W1983256441 doi "https://doi.org/10.1016/j.jmb.2003.11.005" @default.
• W1983256441 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14687577" @default.
• W1983256441 hasPublicationYear "2004" @default.
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