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Updated: May 23, 2026
11:13
Identification of Kinase-substrate Pairs Using High Throughput Screening
Published on: August 29, 2015
The structural basis for control of eukaryotic protein kinases
Jane A Endicott1, Martin E M Noble, Louise N Johnson
1Northern Institute for Cancer Research, Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom.
Annual Review of Biochemistry
|April 10, 2012
Summary
Protein kinases regulate cell processes by adopting active conformations. Understanding their structure reveals mechanisms of activation, including substrate binding and remote docking sites.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Eukaryotic protein kinases are crucial regulators of cellular functions.
- Understanding protein kinase activation mechanisms is vital for cell biology research.
- Structural comparisons offer insights into kinase regulation.
Purpose of the Study:
- To elucidate the structural basis of protein kinase activation.
- To understand the catalytic mechanism of protein kinases.
- To review diverse mechanisms regulating kinase activity.
Main Methods:
- Comparative structural analysis of protein kinase domains.
- Examination of protein kinase-substrate complexes.
- Review of literature on kinase activation mechanisms.
Main Results:
- Active protein kinases adopt a specific conformation upon binding ATP and peptide substrates.
- Remote docking sites are important for substrate recognition in several complexes.
- Multiple activation pathways exist, including phosphorylation, subunit association, scaffolding, and dimerization.
Conclusions:
- Structural insights reveal the catalytic mechanism and active state conformation of protein kinases.
- Diverse mechanisms contribute to the regulation of protein kinase activity.
- Further research into these mechanisms can inform therapeutic strategies.
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