Factor IX

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Human factor IX residues 133-188 (green), residues 227-461 (grey) complex with benzothiophene inhibitor and Ca+2 ions (green) (PDB code 3lc3)

Additional Resources

For additional information, see: Colored & Bioluminescent Proteins
For additional information, see: Hemophilia


References

  1. Spitzer SG, Kuppuswamy MN, Saini R, Kasper CK, Birktoft JJ, Bajaj SP. Factor IXHollywood: substitution of Pro55 by Ala in the first epidermal growth factor-like domain. Blood. 1990 Oct 15;76(8):1530-7. PMID:2169923
  2. Schmidt AE, Bajaj SP. Structure-function relationships in factor IX and factor IXa. Trends Cardiovasc Med. 2003 Jan;13(1):39-45. PMID:12554099
  3. Zhong D, Bajaj MS, Schmidt AE, Bajaj SP. The N-terminal epidermal growth factor-like domain in factor IX and factor X represents an important recognition motif for binding to tissue factor. J Biol Chem. 2002 Feb 1;277(5):3622-31. Epub 2001 Nov 26. PMID:11723140 doi:10.1074/jbc.M111202200
  4. Perona JJ, Craik CS. Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold. J Biol Chem. 1997 Nov 28;272(48):29987-90. PMID:9374470
  5. Ludwig M, Sabharwal AK, Brackmann HH, Olek K, Smith KJ, Birktoft JJ, Bajaj SP. Hemophilia B caused by five different nondeletion mutations in the protease domain of factor IX. Blood. 1992 Mar 1;79(5):1225-32. PMID:1346975
  6. Murav'ev IA, Mar'iasis ED, Starokozhko LE, Chebotarev VV, Krasova TG. [Determination of the biologic availability of preparations for topical use by experimental dermatologic methods] Farmatsiia. 1977 Jul-Aug;26(4):15-9. PMID:902786
  7. Morris DP, Stevens RD, Wright DJ, Stafford DW. Processive post-translational modification. Vitamin K-dependent carboxylation of a peptide substrate. J Biol Chem. 1995 Dec 22;270(51):30491-8. PMID:8530480
  8. Pan LC, Price PA. The propeptide of rat bone gamma-carboxyglutamic acid protein shares homology with other vitamin K-dependent protein precursors. Proc Natl Acad Sci U S A. 1985 Sep;82(18):6109-13. PMID:3875856
  9. Knobloch JE, Suttie JW. Vitamin K-dependent carboxylase. Control of enzyme activity by the "propeptide" region of factor X. J Biol Chem. 1987 Nov 15;262(32):15334-7. PMID:2890628
  10. Knobloch JE, Suttie JW. Vitamin K-dependent carboxylase. Control of enzyme activity by the "propeptide" region of factor X. J Biol Chem. 1987 Nov 15;262(32):15334-7. PMID:2890628
  11. Cheung A, Engelke JA, Sanders C, Suttie JW. Vitamin K-dependent carboxylase: influence of the "propeptide" region on enzyme activity. Arch Biochem Biophys. 1989 Nov 1;274(2):574-81. PMID:2802629
  12. Lin PJ, Jin DY, Tie JK, Presnell SR, Straight DL, Stafford DW. The putative vitamin K-dependent gamma-glutamyl carboxylase internal propeptide appears to be the propeptide binding site. J Biol Chem. 2002 Aug 9;277(32):28584-91. Epub 2002 May 28. PMID:12034728 doi:10.1074/jbc.M202292200
  13. Sanford DG, Kanagy C, Sudmeier JL, Furie BC, Furie B, Bachovchin WW. Structure of the propeptide of prothrombin containing the gamma-carboxylation recognition site determined by two-dimensional NMR spectroscopy. Biochemistry. 1991 Oct 15;30(41):9835-41. PMID:1911775
  14. Lin PJ, Jin DY, Tie JK, Presnell SR, Straight DL, Stafford DW. The putative vitamin K-dependent gamma-glutamyl carboxylase internal propeptide appears to be the propeptide binding site. J Biol Chem. 2002 Aug 9;277(32):28584-91. Epub 2002 May 28. PMID:12034728 doi:10.1074/jbc.M202292200
  15. Furie B, Bouchard BA, Furie BC. Vitamin K-dependent biosynthesis of gamma-carboxyglutamic acid. Blood. 1999 Mar 15;93(6):1798-808. PMID:10068650
  16. Thompson AR. Structure, function, and molecular defects of factor IX. Blood. 1986 Mar;67(3):565-72. PMID:3511981
  17. Stenflo J, Fernlund P, Egan W, Roepstorff P. Vitamin K dependent modifications of glutamic acid residues in prothrombin. Proc Natl Acad Sci U S A. 1974 Jul;71(7):2730-3. PMID:4528109
  18. Furie B, Furie BC. Molecular and cellular biology of blood coagulation. N Engl J Med. 1992 Mar 19;326(12):800-6. PMID:1538724 doi:http://dx.doi.org/10.1056/NEJM199203193261205
  19. Shikamoto Y, Morita T, Fujimoto Z, Mizuno H. Crystal structure of Mg2+- and Ca2+-bound Gla domain of factor IX complexed with binding protein. J Biol Chem. 2003 Jun 27;278(26):24090-4. Epub 2003 Apr 14. PMID:12695512 doi:10.1074/jbc.M300650200
  20. Huang M, Furie BC, Furie B. Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody. J Biol Chem. 2004 Apr 2;279(14):14338-46. Epub 2004 Jan 13. PMID:14722079 doi:10.1074/jbc.M314011200
  21. Golinelli-Pimpaneau B, Gigant B, Bizebard T, Navaza J, Saludjian P, Zemel R, Tawfik DS, Eshhar Z, Green BS, Knossow M. Crystal structure of a catalytic antibody Fab with esterase-like activity. Structure. 1994 Mar 15;2(3):175-83. PMID:8069632
  22. Furie BC, Blumenstein M, Furie B. Metal binding sites of a gamma-carboxyglutamic acid-rich fragment of bovine prothrombin. J Biol Chem. 1979 Dec 25;254(24):12521-30. PMID:500729
  23. Nakagawa T, Tani M, Kita K, Ito M. Preparation of fluorescence-labeled GM1 and sphingomyelin by the reverse hydrolysis reaction of sphingolipid ceramide N-deacylase as substrates for assay of sphingolipid-degrading enzymes and for detection of sphingolipid-binding proteins. J Biochem. 1999 Sep;126(3):604-11. PMID:10467178

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