Protein Kinases: Evolution of Dynamic Regulatory Proteins
By Susan S. Taylor, Alexandr P. Kornev. TIBS -Trends in Biochemical Sciences. Regular ed, 2010
870 citations recorded by the source corpus.
Eukaryotic protein kinases evolved as a family of highly dynamic molecules with strictly organized internal architecture. A single hydrophobic F-helix serves as a central scaffold for assembly of the entire molecule. Two non-consecutive hydrophobic structures termed “Spines” anchor all the elements important for catalysis to the F-helix. They make firm, but flexible, connections within the molecule providing a high level of internal dynamics of the protein kinase. During the course of evolution, protein kinases developed a universal regulatory mechanism associated with a large Activation Segment that can be dynamically folded and unfolded in the course of cell functioning. Protein kinases thus represent a unique, highly dynamic and precisely regulated set of switches that control most biological events in eukaryotic cells.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/75ce8540ba348a6b925f7b5cb5de6698b4ca97b4
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Citations in the corpus
- ERK1/2 MAP kinases: structure, function, and regulation. (2012, methodology): “The catalytic spine of protein kinases consists of residues from the amino-terminal and carboxyterminal lobes that is completed by the adenine moiety of ATP [58].”
- The ErbB/HER family of protein-tyrosine kinases and cancer. (2014, methodology): “Structures of the hydrophobic spines in the active and ormant ErbB1 protein kinase domain Taylor and Kornev [61] and Kornev et al. [52] analyzed the strucures of active and dormant conformations of some two dozen rotein kinases and determined functionally important residues y a local spatial pattern”
- Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition (2012, background): “Compared to other regulatory proteins, kinase activity is controlled by a particularly rich spectrum of mechanisms and these protein undergo extensive structural rearrangements upon activation (Taylor and Kornev, 2010).”