Biochem Biophys Res Commun. 1990 Sep 14;171(2):661-8.

Primary structure of vitamin K-dependent human protein Z.

Sejima H, Hayashi T, Deyashiki Y, Nishioka J, Suzuki K.

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Division of Enzyme Cytology, Institute for Enzyme Research, University of Tokushima, Japan.

Abstract

The primary structure of a vitamin K-dependent human protein Z was determined by a combination of analyses of 41 amino acid residues of the NH2-terminal region and 1265 nucleotide base pairs of a cDNA encoding the residual COOH-terminal part of the protein and the 3' noncoding region. Human protein Z has 360 amino acid residues which is less than that of bovine protein Z containing 396 residues. Human protein Z was composed of an NH2-terminal domain rich in gamma-carboxyglutamic acids, two epidermal growth factor-like domains and a COOH-terminal serine protease-like domain as was bovine protein Z.

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Cited by 11 PubMed Central articles

The role of Ca(2+) ions in the complex assembling of protein Z and Z-dependent protease inhibitor: A structure and dynamics investigation. [Bioinformation. 2012]
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Mechanism of protein-z-mediated inhibition of coagulation factor xa by z-protein-dependent inhibitor: a molecular dynamic approach. [ISRN Hematol. 2012]
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Asproudis I, Felekis TL, Gorezis S, Dova L, Dokou E, Vartholomatos G, Aspiotis M, Kolaitis NI. Open Ophthalmol J. 2009 Apr 28; 3:15-9. Epub 2009 Apr 28.

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