ArticleProteins2014
Solution NMR studies reveal no global flexibility in the catalytic domain of CDC25B.
Article in Proteins, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 7 citations in OpenAlex.
- Identification of the quinolinedione inhibitor binding site in Cdc25 phosphatase B through docking and molecular dynamics simulations.Journal of computer-aided molecular design · 2017Article
- Inhibition of CDC25B phosphatase through disruption of protein-protein interaction.ACS chemical biology · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The CDC25B phosphatase is a critical regulator of the cell cycle and has been validated as an important therapeutic target in cancer. Previous studies using molecular dynamics simulations have concluded that the catalytic domain of CDC25B may experience a significant degree of dynamics or be partially disordered in solution, a finding that has a pronounced impact on the structure-based development of CDC25B inhibitors. We have probed the backbone dynamics of the CDC25B catalytic domain in solution using NMR relaxation experiments and found that the core of the protein is relatively rigid and does not experience any large-scale dynamics over a broad range of time scales. Furthermore, based on residual dipolar coupling measurements we have concluded that the conformation in solution is very similar to that observed in the crystal form. Importantly, these findings rationalize the application of the CDC25B crystal structure in structure-based drug development.
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Registered trials
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