Oncomodulin in Normal and Transformed Cells

  • John P. MacManus
  • Linda M. Brewer
  • Denis Banville
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 269)


The 3-dimensional crystal structure of oncomodulin from X-ray analysis reveals that it is quite similar to that of parvalbumin (F. Ahmed et al., in preparation). Oncomodulin has three domains composed of helix:metal-binding loop:helix arranged in a similar way to parvalbumin (Moews and Kretsinger 1975). This was not unexpected because it was known that oncomodulin and parvalbumin share 50% identical amino acid sequence, and an additional 30% conservative residue replacement (MacManus et al., 1987). Also both the circular dichroic and proton NMR spectra suggested the existence of great similarity of secondary structure (MacManus et al., 1984; Williams et al., 1987).


Circular Dichroic Leydig Cell Tumor Baby Hamster Kidney Cell Ectoplacental Cone Mammalian Embryonic Development 
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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • John P. MacManus
    • 1
  • Linda M. Brewer
    • 1
  • Denis Banville
    • 2
  1. 1.Division of Biological SciencesNational Research CouncilOttawaCanada
  2. 2.BioTechnology Research InstituteNational Research CouncilMontrealCanada

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