[Latent periodicity of serine-threonine and tyrosine protein kinases and another protein families].
We identified latent periodicity in catalytic domains of approximately 85% of serine/threonine and tyrosine protein kinases. Similar results were obtained for other 22 protein 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 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.
Laskin
A A
AA
Kudriashev
N A
NA
Skriabin
K G
KG
Korotkov
E V
EV
D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D019295:Computational Biology; D030562:Databases, Protein; D006801:Humans; D008969:Molecular Sequence Data; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry*; D011505:Protein-Tyrosine Kinases / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D011505:Protein-Tyrosine Kinases; D017346:Protein Serine-Threonine Kinases