Site-directed mutagenesis at p6 in heparin cofactorii creates a thrombin-inhibitory serpin that is resistant to neutrophil elastaseinac1tvation

Heparin cofactor II (HCII) is a member of the serine protease inhibitor, or serpins, family of proteins. It inhibits thrombin in plasma by providing a bait -like substrate motif on a surface-exposed reactive center loop (RCL), and subsequently forming denaturation-resistant inhibitory complexes with the protease. While thrombin acts a,s a target protease with HCII, neutrophil elastase (NE), another serine protease, reacts with HCII within the …