Latent periodicity of serine-threonine and tyrosine protein kinases and other protein families.
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.
Bioengineering Center of Russian Academy of Sciences, Prospect 60-tya Oktyabrya, 7/1, 117312 Moscow, Russia. anti@victoria.biengi.ac.ru
Andrew A
AA
Laskin
Nikolay A
NA
Kudryashov
Konstantin G
KG
Skryabin
Eugene V
EV
Korotkov
D000465:Algorithms; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D020134:Catalytic Domain; D008969:Molecular Sequence Data; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry*; D011505:Protein-Tyrosine Kinases / Q000737:chemistry*
D011505:Protein-Tyrosine Kinases; D017346:Protein Serine-Threonine Kinases