Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase

Autor: Toni Gestone Parmer, F. Joseph Germino, Maxim V. Dorovkov, Hediye Erdjument-Bromage, Charmaine E. Mendola, Paul Tempst, Michael D. Ward, Karen S. Pavur, William N. Hait, C. Robert Prostko, Martin Wiedmann, Alexey G. Ryazanov
Rok vydání: 1997
Předmět:
Zdroj: Proceedings of the National Academy of Sciences. 94:4884-4889
ISSN: 1091-6490
0027-8424
DOI: 10.1073/pnas.94.10.4884
Popis: The several hundred members of the eukaryotic protein kinase superfamily characterized to date share a similar catalytic domain structure, consisting of 12 conserved subdomains. Here we report the existence and wide occurrence in eukaryotes of a protein kinase with a completely different structure. We cloned and sequenced the human, mouse, rat, and Caenorhabditis elegans eukaryotic elongation factor-2 kinase (eEF-2 kinase) and found that with the exception of the ATP-binding site, they do not contain any sequence motifs characteristic of the eukaryotic protein kinase superfamily. Comparison of different eEF-2 kinase sequences reveals a highly conserved region of ≈200 amino acids which was found to be homologous to the catalytic domain of the recently described myosin heavy chain kinase A (MHCK A) from Dictyostelium. This suggests that eEF-2 kinase and MHCK A are members of a new class of protein kinases with a novel catalytic domain structure.
Databáze: OpenAIRE