Structural Insights into Cdk5 Activation by a Neuronal Cdk5 Activator
Copyright policy )Structural Insights into Cdk5 Activation by a Neuronal Cdk5 Activator
Although Cdk5 shows high sequence identity to Cdk1 and Cdk2, it can be fully activated by its neuronal activators p35/p25(nck5a) and p39(nck5ai) in a phosphorylation-independent manner. To understand structural basis of the Cdk5/p25(nck5a) activation, the complex is modelled to assume either an obstructed or an opened conformation based on X-ray structures of the unphosphorylated or the phosphorylated Cdk2/cyclin A complex, respectively. Comparison and analysis of the two models, along with mutagenesis studies of p25(nck5a), suggest that the opened form represents more closely the structure of active Cdk5/p25(nck5a). The results provide a rationale basis for understanding the phosphorylation-independent activation of Cdk5/p25(nck5a).
- Hong Kong Polytechnic University China (People's Republic of)
- Institute of Molecular and Cell Biology Singapore
- Agency for Science, Technology and Research Singapore
- Hong Kong University of Science and Technology (香港科技大學) China (People's Republic of)
Models, Molecular, Protein Conformation, Cdk5, Molecular Sequence Data, Enzyme Activators, Nerve Tissue Proteins, Crystallography, X-Ray, Substrate Specificity, Mice, Animals, Comparative homology modelling, Amino Acid Sequence, Phosphorylation, Neurons, Sequence Homology, Amino Acid, Phosphorylation-independent activation, Cyclin-Dependent Kinase 5, Hydrogen Bonding, Cyclin-Dependent Kinases, Recombinant Proteins, Enzyme Activation, Mutagenesis, Site-Directed, Nck5a
Models, Molecular, Protein Conformation, Cdk5, Molecular Sequence Data, Enzyme Activators, Nerve Tissue Proteins, Crystallography, X-Ray, Substrate Specificity, Mice, Animals, Comparative homology modelling, Amino Acid Sequence, Phosphorylation, Neurons, Sequence Homology, Amino Acid, Phosphorylation-independent activation, Cyclin-Dependent Kinase 5, Hydrogen Bonding, Cyclin-Dependent Kinases, Recombinant Proteins, Enzyme Activation, Mutagenesis, Site-Directed, Nck5a
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