Factor Xa

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Human factor X heavy chain (grey) and light chain (green) complex with pyrrolydine derivative inhibitor and Ca+2 ions (green) (PDB code 2pr3)

3D structures of factor Xa

Updated on 11-May-2017

Additional Resources

For additional information, see: Hemophilia

References

  1. 1.0 1.1 Greer, John (2008). Wintrobe's Clinical Hematology, p. 545-546. Lippincott Williams & Wilkins. ISBN 0781765072.
  2. 2.0 2.1 Department of Chemistry, University of Maine, Orono, ME. http://chemistry.umeche.maine.edu/CHY252/Peptidase3.html
  3. Padmanabhan K, Padmanabhan KP, Tulinsky A, Park CH, Bode W, Huber R, Blankenship DT, Cardin AD, Kisiel W. Structure of human des(1-45) factor Xa at 2.2 A resolution. J Mol Biol. 1993 Aug 5;232(3):947-66. PMID:8355279 doi:http://dx.doi.org/10.1006/jmbi.1993.1441
  4. Friedman PA, Przysiecki CT. Vitamin K-dependent carboxylation. Int J Biochem. 1987;19(1):1-7. PMID:3106112
  5. Vermeer C. Gamma-carboxyglutamate-containing proteins and the vitamin K-dependent carboxylase. Biochem J. 1990 Mar 15;266(3):625-36. PMID:2183788
  6. Price PA, Fraser JD, Metz-Virca G. Molecular cloning of matrix Gla protein: implications for substrate recognition by the vitamin K-dependent gamma-carboxylase. Proc Natl Acad Sci U S A. 1987 Dec;84(23):8335-9. PMID:3317405
  7. Freedman SJ, Furie BC, Furie B, Baleja JD. Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy. J Biol Chem. 1995 Apr 7;270(14):7980-7. PMID:7713897
  8. Freedman SJ, Blostein MD, Baleja JD, Jacobs M, Furie BC, Furie B. Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX. J Biol Chem. 1996 Jul 5;271(27):16227-36. PMID:8663165
  9. Morita T, Jackson CM. Preparation and properties of derivatives of bovine factor X and factor Xa from which the gamma-carboxyglutamic acid containing domain has been removed. J Biol Chem. 1986 Mar 25;261(9):4015-23. PMID:3512564
  10. Muskavitch MA, Hoffmann FM. Homologs of vertebrate growth factors in Drosophila melanogaster and other invertebrates. Curr Top Dev Biol. 1990;24:289-328. PMID:2116263
  11. Ohlin AK, Linse S, Stenflo J. Calcium binding to the epidermal growth factor homology region of bovine protein C. J Biol Chem. 1988 May 25;263(15):7411-7. PMID:3259233
  12. 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. 1992 Sep 25;267(27):19642-9. PMID:1527084
  13. Persson E, Hogg PJ, Stenflo J. Effects of Ca2+ binding on the protease module of factor Xa and its interaction with factor Va. Evidence for two Gla-independent Ca(2+)-binding sites in factor Xa. J Biol Chem. 1993 Oct 25;268(30):22531-9. PMID:8226763
  14. Persson E, Selander M, Linse S, Drakenberg T, Ohlin AK, Stenflo J. Calcium binding to the isolated beta-hydroxyaspartic acid-containing epidermal growth factor-like domain of bovine factor X. J Biol Chem. 1989 Oct 5;264(28):16897-904. PMID:2789221
  15. Hopfner KP, Kopetzki E, Kresse GB, Bode W, Huber R, Engh RA. New enzyme lineages by subdomain shuffling. Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):9813-8. PMID:9707558
  16. Factor X. Wikipedia
  17. Serine Protease. Wikipedia
  18. 18.0 18.1 Hedstrom L. Serine protease mechanism and specificity. Chem Rev. 2002 Dec;102(12):4501-24. PMID:12475199
  19. 19.0 19.1 Rai R, Sprengeler PA, Elrod KC, Young WB. Perspectives on factor Xa inhibition. Curr Med Chem. 2001 Feb;8(2):101-19. PMID:11172669
  20. www.bmolchem.wisc.edu/
  21. 21.0 21.1 Bachovchin, W. Contributions of NMR spectroscopy to the study of hydrogen bonds in serine protease active sites. Magnetic Resonance in Chemistry; (2001); 39(Spec. Issue); 199-213.
  22. Bachovchin WW. 15N NMR spectroscopy of hydrogen-bonding interactions in the active site of serine proteases: evidence for a moving histidine mechanism. Biochemistry. 1986 Nov 18;25(23):7751-9. PMID:3542033
  23. Brady K, Wei AZ, Ringe D, Abeles RH. Structure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitors. Biochemistry. 1990 Aug 21;29(33):7600-7. PMID:2271520
  24. Frey PA, Whitt SA, Tobin JB. A low-barrier hydrogen bond in the catalytic triad of serine proteases. Science. 1994 Jun 24;264(5167):1927-30. PMID:7661899
  25. Frey, Perry A. Strong hydrogen bonding in chymotrypsin and other serine proteases. Journal of Physical Organic Chemistry (2004), 17(6-7), 511-520.
  26. 26.0 26.1 Fuhrmann CN, Daugherty MD, Agard DA. Subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis. J Am Chem Soc. 2006 Jul 19;128(28):9086-102. PMID:16834383 doi:http://dx.doi.org/10.1021/ja057721o
  27. Kuhn P, Knapp M, Soltis SM, Ganshaw G, Thoene M, Bott R. The 0.78 A structure of a serine protease: Bacillus lentus subtilisin. Biochemistry. 1998 Sep 29;37(39):13446-52. PMID:9753430 doi:10.1021/bi9813983

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