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BMCBI
2007

Identifying allosteric fluctuation transitions between different protein conformational states as applied to Cyclin Dependent Ki

8 years 11 months ago
Identifying allosteric fluctuation transitions between different protein conformational states as applied to Cyclin Dependent Ki
Background: The mechanisms underlying protein function and associated conformational change are dominated by a series of local entropy fluctuations affecting the global structure yet are mediated by only a few key residues. Transitional Dynamic Analysis (TDA) is a new method to detect these changes in local protein flexibility between different conformations arising from, for example, ligand binding. Additionally, Positional Impact Vertex for Entropy Transfer (PIVET) uses TDA to identify important residue contact changes that have a large impact on global fluctuation. We demonstrate the utility of these methods for Cyclin-dependent kinase 2 (CDK2), a system with crystal structures of this protein in multiple functionally relevant conformations and experimental data revealing the importance of local fluctuation changes for protein function. Results: TDA and PIVET successfully identified select residues that are responsible for conformation specific regional fluctuation in the activatio...
Jenny Gu, Philip E. Bourne
Added 08 Dec 2010
Updated 08 Dec 2010
Type Journal
Year 2007
Where BMCBI
Authors Jenny Gu, Philip E. Bourne
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