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Thromb Haemost 2004; 92(05): 1161-1163
DOI: 10.1055/s-0037-1614297
Letters to the Editor
Schattauer GmbH

Two new factor X mutations (Pro382Leu and Phe356Cys) associated with low activity and low antigen levels

Susan Deam
1   Departments of Haematology and Clinical Chemistry, Queen’s Medical Centre, Nottingham, UK
,
James Uprichard
2   Haemophilia Centre and Haemostasis Unit, Department of Haematology, Royal Free and University College Medical School, London, UK
,
Julian T. Eaton
3   Department of Biochemistry and Molecular Biology, Royal Free and University College Medican School, University College London, London, UK
,
Stephen J. Perkins
3   Department of Biochemistry and Molecular Biology, Royal Free and University College Medican School, University College London, London, UK
,
Hasmukh Dasani
4   The Arthur Bloom Haemophilia Centre, University Hospital Wales, Cardiff, Wales
,
John Hanley
5   Newcastle Haemophilia Centre, Royal Victoria Infirmary, Newcastle upon Tyne, UK
,
Gerard Dolan
1   Departments of Haematology and Clinical Chemistry, Queen’s Medical Centre, Nottingham, UK
› Author AffiliationsFinancial support: We thank the Special Trustees of the University Hospital Nottingham for their support. James Uprichard gratefully acknowledges the financial support of the Katharine Dormandy Trust for Haemophilia and Allied Disorders. Julian Eaton and Stephen Perkins are supported by the Wellcome Trust.
Further Information

Publication History

Received 02 February 2004

Accepted after revision 06 September 2004

Publication Date:
14 December 2017 (online)

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  • References

  • 1 Uprichard J, Perry DJ. Factor X deficiency. Blood Reviews 2002; 16: 97-110.
    CrossrefPubMedSearch in Google Scholar
  • 2 Zivelin A, Salomon O, Kenet G. et al. Cys61-stop is the first identified nonsense mutation in the factor X gene causing severe factor X deficiency in 3 unrelated homozygotes of Arab origin. J Thromb Haemost. 2003 suppl.
    PubMedSearch in Google Scholar
  • 3 Padmanabhan K, Padmanabhan KP, Tulinsky A. et al. Structure of human des(1-45) factor Xa at 2.2 A resolution. J Mol Biol 1993; 232: 947-66.
    CrossrefPubMedSearch in Google Scholar
  • 4 Maignan S, Guilloteau JP, Pouzieux S. et al. Crystal structures of human factor Xa complexed with potent inhibitors. J Med Chem 2000; 43: 3226-32.
    CrossrefPubMedSearch in Google Scholar
  • 5 Kamata K, Kawamoto H, Honma T. et al. Structural basis for chemical inhibition of human blood coagulation factor Xa. P Natl Acad Sci USA 1998; 95: 6630-5.
    CrossrefPubMedSearch in Google Scholar
  • 6 Leytus SP, Foster DC, Kurachi K. et al. Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C. Biochemistry 1986; 25: 5098-102.
    CrossrefPubMedSearch in Google Scholar
  • 7 Jenkins PV, Pasi KJ, Perkins SJ. Molecular modeling of ligand and mutation sites of the type A domains of human von Willebrand factor and their relevance to von Willebrand’s disease. Blood 1998; 91: 2032-44.
    PubMedSearch in Google Scholar
  • 8 Deam S, Srinivasan N, Westby J. et al. F X Nottingham and FX Taunton: Two novel mutations resulting in loss of functional activity and an interpretation using molecular modelling. J Thromb Haemost 2001; 85: 265-9.
    Thieme ConnectPubMedSearch in Google Scholar
  • 9 Altschul SF, Madden TL, Schaffer AA. et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997; 25: 3389-402.
    CrossrefPubMedSearch in Google Scholar
  • 10 Messier TL, Pittman DD, Long GL. et al. Cloning and expression in COS-1 cells of a full-length cDNA encoding human coagulation Factor X. Gene 1991; 99: 291-4.
    CrossrefPubMedSearch in Google Scholar
  • 11 Higgins DG, Bleasby AJ, Fuchs R. CLUSTAL V: improved software for multiple sequence alignment. Comput Appl Biosci 1992; 08: 189-91.
    PubMedSearch in Google Scholar
  • 12 Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983; 22: 2577-637.
    CrossrefPubMedSearch in Google Scholar
  • 13 Lee B, Richards FM. The interpretation of protein structures: estimation of static accessibility. J Mol Biol 1971; 55: 379-400.
    CrossrefPubMedSearch in Google Scholar
  • 14 Sali A, Blundell TL. Definition of general topological equivalence in protein structures. A procedure involving comparison of properties and relationships through simulated annealing and dynamic programming. J Mol Biol 1990; 212: 403-28.
    CrossrefPubMedSearch in Google Scholar
  • 15 Perkins SJ, Smith KF. Identity of the putative serine-proteinase fold in proteins of the complement system with nine relevant crystal structures. Biochem J 1993; 295: 109-14.
    CrossrefPubMedSearch in Google Scholar
  • 16 MacArthur MW, Thornton JM. Influence of proline residues on protein conformation. J Mol Biol 1991; 218: 397-412.
    CrossrefPubMedSearch in Google Scholar
  • 17 Creighton TE. Proteins: Structures and Molecular Properties. New York: W.H. Freeman; 1993
  • 18 Rudolph A, Mullane MP, Porche-Sorbet R. et al. Factor X St. Louis II. 1996. Identification of a glycine substitution at residue 7 and characterization of the recombinant protein. J Biol Chem 1996; 271: 28601-6.
    CrossrefPubMedSearch in Google Scholar