Conservation, Variability and the Modeling of Active Protein Kinases
2007

Modeling Protein Kinases

Sample size: 14 publication 10 minutes Evidence: moderate

Author Information

Author(s): James D. R. Knight, Bin Qian, David Baker, Rashmi Kothary

Primary Institution: Molecular Medicine Program, Ottawa Health Research Institute, Ottawa, Ontario, Canada

Hypothesis

Understanding the structural biology of protein kinases is necessary for designing high-quality inhibitors for cell biology and disease therapy.

Conclusion

The study provides insights into the conservation and variability of protein kinases, which can guide the design of specific inhibitors.

Supporting Evidence

  • Protein kinases are crucial for cell behavior and are potential drug targets for various diseases.
  • The study highlights flaws in traditional kinase drug design, emphasizing the need for a new approach.
  • Understanding residue conservation and variability can aid in the design of specific inhibitors.
  • The study presents a consensus structure that can guide structure prediction for protein kinases.

Takeaway

This study looks at how protein kinases work and how we can create better drugs to target them by understanding their structure.

Methodology

The study used a novel structural alignment algorithm to analyze active-conformation protein kinases and their variability.

Limitations

The study primarily focuses on a limited number of active-conformation kinases and may not represent all kinases.

Digital Object Identifier (DOI)

10.1371/journal.pone.0000982

Want to read the original?

Access the complete publication on the publisher's website

View Original Publication