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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)

Abstract

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).

Keywords

Circular Dichroic Leydig Cell Tumor Baby Hamster Kidney Cell Ectoplacental Cone Mammalian Embryonic Development 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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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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