Protein kinases interactions

Knauf, U., Tschopp, C., and Gram, H. (2001). Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2. Mol. Cell. Biol. 21, 5500-5511. 

Cohen, S., Carpenter, G., and King, L., Jr. (1980). Epidermal growth factor-receptor-protein kinase interactions. Co-purification of receptor and epidermal growth factor-enhanced phosphorylation activity. J. Biol. Chem. 255, 4834-4842. 

Herberg, F. W., Zimmermann, B. (1999). Analysis of protein kinase interactions using biomolecular interaction analysis. In Hardie, D. G. (Ed.), Protein Phosphorylation - A Practical Approach. Oxford University Press, pp. 335-371. 

MAPKAP-K MAPK-activated protein kinase MNK mitogen-activated protein kinase-interacting kinase MSK mitogen- and stress-activated protein kinase PRAK p38-regulated/activated protein kinase RSK 90kDa-ribosomal S6 kinase. 

Li, X, J. Wen, K.A. Lease, XT. Doke, F.E. Tax and XC. Walker (2002). BAKl, an Arabidopsis LRR receptor-like protein kinase, interacts with BRIl and modulates brassinosteroid signalling. Cell 110,213-222. 

Thiazolo[4,5-d]pyrimidine derivatives e.g. 206 are prepared as inhibitors of ATP-protein kinase interactions [128],... 

A number of issues need to be addressed before this method will become a routine tool applicable to problems as the conformational equilibrium of protein kinase. E.g. the accuracy of the force field, especially the combination of Poisson-Boltzmann forces and molecular mechanics force field, remains to be assessed. The energy surface for the opening of the two kinase domains in Pig. 2 indicates that intramolecular noncovalent energies are overestimated compared to the interaction with solvent. 

The spatial and steric requirements for high affinity binding to protein kinase C (PKC), a macromolecule that has not yet been crystallized, were determined. Protein kinase C plays a critical role in cellular signal transduction and is in part responsible for cell differentiation. PKC was identified as the macromolecular target for the potent tumor-promoting phorbol esters (25). The natural agonists for PKC are diacylglycerols (DAG) (26). The arrows denote possible sites of interaction. 

Src tyrosine kinase contains both an SH2 and an SH3 domain linked to a tyrosine kinase unit with a structure similar to other protein kinases. The phosphorylated form of the kinase is inactivated by binding of a phosphoty-rosine in the C-terminal tail to its own SH2 domain. In addition the linker region between the SH2 domain and the kinase is bound in a polyproline II conformation to the SH3 domain. These interactions lock regions of the active site into a nonproductive conformation. Dephosphorylation or mutation of the C-terminal tyrosine abolishes this autoinactivation. 

Phosphorylation is a common method of regulation. As described above, SH2 domains bind to phosphorylated tyrosine residues. Conversely, phosphorylation of serines and threonines proximal to SH3 and PDZ domains uncouples them from their target motifs. Therefore modulation of protein kinase activity in cells regulates interactions between adaptor proteins and their target proteins. 

Interactions with the cytoskeleton seem to be responsible for the processing and the targeting of the Na+/fC+-ATPase to the appropriate compartment structures. Protein kinases are considered to play an essential role in modulation of the sodium pump. 

AChE-R (in purple) Naturally rare, stress-induced variant, which lacks a hydrophobic domain and is incapable of binding to ColQ or PRiMA. Therefore, it remains soluble, and its secreted form shows greater mobility than AChE-S. AChE-R can intra-cellularly interact through its C-terminal tail with the Protein Kinase C Receptor RACK1, a scaffold protein which modifies multiple cellular processes. 

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