[1]
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NUCLEOTIDE SEQUENCE [MRNA] OF 1-487.
DOI=10.1093/nar/12.11.4481; PubMed=6330671 [NCBI, ExPASy, EBI, Israel, Japan]
Fung M.R.,
Campbell R.M.,
McGillivray R.T.A.;
"Blood coagulation factor X mRNA encodes a single polypeptide chain containing a prepro leader sequence.";
Nucleic Acids Res. 12:4481-4492(1984).
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[2]
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PROTEIN SEQUENCE OF 41-180.
DOI=10.1021/bi00545a009; PubMed=6766735 [NCBI, ExPASy, EBI, Israel, Japan]
Enfield D.L.,
Ericsson L.H.,
Fujikawa K.,
Walsh K.A.,
Neurath H.,
Titani K.;
"Amino acid sequence of the light chain of bovine factor X1 (Stuart factor).";
Biochemistry 19:659-667(1980).
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[3]
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SEQUENCE REVISION TO 103.
DOI=10.1016/0006-291X(83)90961-0; PubMed=6688526 [NCBI, ExPASy, EBI, Israel, Japan]
McMullen B.A.,
Fujikawa K.,
Kisiel W.;
"The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens.";
Biochem. Biophys. Res. Commun. 115:8-14(1983).
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[4]
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PROTEIN SEQUENCE OF 183-492, GLYCOSYLATION AT ASN-218 AND THR-485, AND DISULFIDE BONDS.
PubMed=1059093 [NCBI, ExPASy, EBI, Israel, Japan]
Titani K.,
Fujikawa K.,
Enfield D.L.,
Ericsson L.H.,
Walsh K.A.,
Neurath H.;
"Bovine factor X1 (Stuart factor): amino-acid sequence of heavey chain.";
Proc. Natl. Acad. Sci. U.S.A. 72:3082-3086(1975).
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[5]
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PROTEIN SEQUENCE OF 183-233, AND GLYCOSYLATION AT THR-208.
PubMed=8243461 [NCBI, ExPASy, EBI, Israel, Japan]
Inoue K.,
Morita T.;
"Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X.";
Eur. J. Biochem. 218:153-163(1993).
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[6]
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ACTIVE SITE.
DOI=10.1021/bi00776a004; PubMed=4264286 [NCBI, ExPASy, EBI, Israel, Japan]
Titani K.,
Hermodson M.A.,
Fujikawa K.,
Ericsson L.H.,
Walsh K.A.,
Neurath H.,
Davie E.W.;
"Bovine factor X 1a (activated Stuart factor). Evidence of homology with mammalian serine proteases.";
Biochemistry 11:4899-4903(1972).
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[7]
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PROTEOLYTIC PROCESSING.
PubMed=1059122 [NCBI, ExPASy, EBI, Israel, Japan]
Fujikawa K.,
Titani K.,
Davie E.W.;
"Activation of bovine factor X (Stuart factor): conversion of factor Xa-alpha to factor Xa-beta.";
Proc. Natl. Acad. Sci. U.S.A. 72:3359-3363(1975).
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[8]
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CALCIUM-BINDING DATA.
PubMed=6546930 [NCBI, ExPASy, EBI, Israel, Japan]
Sugo T.,
Bjoerk I.,
Holmgren A.,
Stenflo J.;
"Calcium-binding properties of bovine factor X lacking the gamma-carboxyglutamic acid-containing region.";
J. Biol. Chem. 259:5705-5710(1984).
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[9]
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SULFATION.
PubMed=3949800 [NCBI, ExPASy, EBI, Israel, Japan]
Morita T.,
Jackson C.M.;
"Localization of the structural difference between bovine blood coagulation factors X1 and X2 to tyrosine 18 in the activation peptide.";
J. Biol. Chem. 261:4008-4014(1986).
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[10]
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STRUCTURE BY NMR OF 85-126.
DOI=10.1021/bi00487a018; PubMed=2261466 [NCBI, ExPASy, EBI, Israel, Japan]
Selander M.,
Persson E.,
Stenflo J.,
Drakenberg T.;
"1H NMR assignment and secondary structure of the Ca2(+)-free form of the amino-terminal epidermal growth factor like domain in coagulation factor X.";
Biochemistry 29:8111-8118(1990).
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[11]
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STRUCTURE BY NMR OF 85-126.
DOI=10.1021/bi00141a004; PubMed=1627540 [NCBI, ExPASy, EBI, Israel, Japan]
Ullner M.,
Selander M.,
Persson E.,
Stenflo J.,
Drakenberg T.,
Teleman O.;
"Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding.";
Biochemistry 31:5974-5983(1992).
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[12]
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STRUCTURE BY NMR OF 85-126.
PubMed=1527084 [NCBI, ExPASy, EBI, Israel, Japan]
Selander-Sunnerhagen M.,
Ullner M.,
Persson E.,
Teleman O.,
Stenflo J.,
Drakenberg T.;
"How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X.";
J. Biol. Chem. 267:19642-19649(1992).
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[13]
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STRUCTURE BY NMR OF 41-126.
DOI=10.1021/bi960633j; PubMed=8794734 [NCBI, ExPASy, EBI, Israel, Japan]
Sunnerhagen M.,
Olah G.A.,
Stenflo J.,
Forsen S.,
Drakenberg T.,
Trewhella J.;
"The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study.";
Biochemistry 35:11547-11559(1996).
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