Latent Periodicity of Many Domains in Protein Sequences Reflects Their Structure, Function, and Evolution

  • A. A. Laskin
  • E. V. Korotkov
  • N. A. Kudryashov

Abstract

We have analyzed many protein sequences for the presence of latent periodicity common for their functionally identical sites. As a result, we found that Rossman-like domains of TPP-binding enzymes, ATP synthases, and pyridoxal phosphate-dependent enzymes as well as many other α/β-proteins, such as dethiobiotin synthases, have latently periodic structure. We also identified the periodicity pattern responsible for formation of parallel n-barrel in a number of enzymes. Possible relationships of regular structures and latent periodicity are also discussed.

Key words

periodicity repeats profile analysis Rossman-like domains regular structures molecular evolution duplication structure-function relationship 

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Copyright information

© Springer Science+Business Media New York 2004

Authors and Affiliations

  • A. A. Laskin
    • 1
  • E. V. Korotkov
    • 1
  • N. A. Kudryashov
    • 2
  1. 1.Bioengineering CenterRussian Academy of SciencesMoscowRussia
  2. 2.Moscow Engineering & Physics InstituteMoscowRussia

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