ArticleBiochimica et biophysica acta2014
Characterization of the protein Z-dependent protease inhibitor interactive-sites of protein Z.
Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Human Protein Z as the Second Known Heme-Binding Protein from the Endogenous Blood Coagulation Inhibitor System.Chembiochem : a European journal of chemical biology · 2026Article
- Loss of protein C vs protein S results in discrepant thrombotic phenotypes.Blood advances · 2025Article
- The serine protease homolog spheroide is involved in sensing of pathogenic Gram-positive bacteria.PloS one · 2017Article
- Phosphatidylserine and Phosphatidylethanolamine Bind to Protein Z Cooperatively and with Equal Affinity.PloS one · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
backgroundProtein Z (PZ) has been reported to promote the inactivation of factor Xa (FXa) by PZ-dependent protease inhibitor (ZPI) by about three orders of magnitude. Previously, we prepared a chimeric PZ in which its C-terminal pseudo-catalytic domain was grafted on FX light-chain (Gla and EGF-like domains) (PZ/FX-LC). Characterization of PZ/FX-LC revealed that the ZPI interactive-site is primarily located within PZ pseudo-catalytic domain. Nevertheless, the cofactor function and apparent Kd of PZ/FX-LC for interaction with ZPI remained impaired ~6-7-fold, suggesting that PZ contains a ZPI interactive-site outside pseudo-catalytic domain. X-ray structural data indicates that Tyr-240 of ZPI interacts with EGF2-domain of PZ. Structural data further suggests that 3 other ZPI surface loops make salt-bridge interactions with PZ pseudo-catalytic domain. To identify ZPI interactive-sites on PZ, we grafted the N-terminal EGF2 subdomain of PZ onto PZ/FX-LC chimera (PZ-EGF2/FX-LC) and also generated two compensatory charge reversal mutants of PZ pseudo-catalytic domain (Glu-244 and Arg-212) and ZPI surface loops (Lys-239 and Asp-293).
methodsPZ chimeras were expressed in mammalian cells and ZPI derivatives were expressed in Escherichia coli.
resultsThe PZ EGF2 subdomain fusion restored the defective cofactor function of PZ/FX-LC. The activities of PZ and ZPI mutants were all impaired if assayed individually, but partially restored if the compensatory charge reversal mutants were used in the assay.
conclusionsPZ EGF2 subdomain constitutes an interactive-site for ZPI. Data with compensatory charge reversal mutants validates structural data that the identified residues are part of interactive-sites. GENERAL SIGNIFICANCE: Insight is provided into mechanisms through which specificity of ZPI-PZ-FXa complex formation is determined.
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