ArticleScientific reports2020
Role of the activation peptide in the mechanism of protein C activation.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Human Genetic Analysis Reveals Circulating Alpha-1 Antitrypsin Level as a Protective Factor in Sepsis.medRxiv : the preprint server for health sciences · 2026Article
- Modifications of the Prothrombin Active Site S4 Subpocket Confer Resistance to Dabigatran.Thrombosis and haemostasis · 2026Article
- [Analysis of two cases of hereditary protein C deficiency causing venous thrombosis].Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi · 2025Article
- Molecular and clinical characterization of two independent Chinese families with protein C deficiency.Annals of hematology · 2025Article
- Platelets at the intersection of inflammation and coagulation in the APC-mediated response to myocardial ischemia/reperfusion injury.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024Review
- Thrombin has dual trypsin-like and chymotrypsin-like specificity.Journal of thrombosis and haemostasis : JTH · 2024Article
- Unraveling the Reaction Mechanism of Russell's Viper Venom Factor X Activator: A Paradigm for the Reactivity of Zinc Metalloproteinases?Journal of chemical information and modeling · 2023Article
- Comparative sequence analysis of vitamin K-dependent coagulation factors.Journal of thrombosis and haemostasis : JTH · 2022Article
- The active site region plays a critical role in NaThe Journal of biological chemistry · 2022Article
- Zymogen and activated protein C have similar structural architecture.The Journal of biological chemistry · 2020Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein C is a natural anticoagulant activated by thrombin in a reaction accelerated by the cofactor thrombomodulin. The zymogen to protease conversion of protein C involves removal of a short activation peptide that, relative to the analogous sequence present in other vitamin K-dependent proteins, contains a disproportionately high number of acidic residues. Through a combination of bioinformatic, mutagenesis and kinetic approaches we demonstrate that the peculiar clustering of acidic residues increases the intrinsic disorder propensity of the activation peptide and adversely affects the rate of activation. Charge neutralization of the acidic residues in the activation peptide through Ala mutagenesis results in a mutant activated by thrombin significantly faster than wild type. Importantly, the mutant is also activated effectively by other coagulation factors, suggesting that the acidic cluster serves a protective role against unwanted proteolysis by endogenous proteases. We have also identified an important H-bond between residues T176 and Y226 that is critical to transduce the inhibitory effect of Ca
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