Analysis of the human kinome using methods including fold recognition reveals two novel kinases.
|Title||Analysis of the human kinome using methods including fold recognition reveals two novel kinases.|
|Publication Type||Journal Article|
|Year of Publication||2008|
|Authors||Briedis KM, Starr A, Bourne PE|
|Keywords||Amino Acid Sequence, Computational Biology, Humans, Protein Conformation, Protein Kinases, Proteins, Proteome, Software|
BACKGROUND: Protein sequence similarity is a commonly used criterion for inferring the unknown function of a protein from a protein of known function. However, proteins can diverge significantly over time such that sequence similarity is difficult, if not impossible, to find. In some cases, a structural similarity remains over long evolutionary time scales and once detected can be used to predict function.
METHODOLOGY/PRINCIPAL FINDINGS: Here we employed a high-throughput approach to assign structural and functional annotation to the human proteome, focusing on the collection of human protein kinases, the human kinome. We compared human protein sequences to a library of domains from known structures using WU-BLAST, PSI-BLAST, and 123D. This approach utilized both sequence comparison and fold recognition methods. The resulting set of potential protein kinases was cross-checked against previously identified human protein kinases, and analyzed for conserved kinase motifs.
CONCLUSIONS/SIGNIFICANCE: We demonstrate that our structure-based method can be used to identify both typical and atypical human protein kinases. We also identify two potentially novel kinases that contain an interesting combination of kinase and acyl-CoA dehydrogenase domains.
|Alternate Title||PLoS ONE|