Latent periodicity of serine-threonine and tyrosine protein kinases and other protein families

Authors:
Andrew A. Laskin;Nikolay A. Kudryashov;Konstantin G. Skryabin;Eugene V. Korotkov
Affiliations:
Bioengineering Center of Russian Academy of Sciences, Prospect 60-tya Oktyabrya, 7/1, 117312 Moscow, Russia and Moscow Physical Engineering Institute, Kashirskoe Shosse 31, 115409 Moscow, Russia;Moscow Physical Engineering Institute, Kashirskoe Shosse 31, 115409 Moscow, Russia;Bioengineering Center of Russian Academy of Sciences, Prospect 60-tya Oktyabrya, 7/1, 117312 Moscow, Russia;Bioengineering Center of Russian Academy of Sciences, Prospect 60-tya Oktyabrya, 7/1, 117312 Moscow, Russia and Moscow Physical Engineering Institute, Kashirskoe Shosse 31, 115409 Moscow, Russia
Venue:
Computational Biology and Chemistry
Year:
2005

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Abstract

We identified latent periodicity in catalytic domains of approximately 85% of annotated serine-threonine and tyrosine protein kinases. Similar results were obtained for other 22 protein families and domains. We also designed the method of noise decomposition, which is aimed to distinguish between different periodicity types of the same period length. The method is to be used in conjunction with the method of cyclic profile alignment, and this combination is able to reveal structure-related or function-related patterns of latent periodicity. Possible origins of the periodic structure of protein kinase active sites are discussed. Summarizing, we presume that latent periodicity is the common property of many catalytic protein domains.