Focal adhesion kinase (FAK) is a component of focal adhesion sites, which plays a crucial role in cell di erentiation and motility. Using molecular dynamic simulations, we observed that binding of the phospho-inositide phosphatidylinsositol-4,5-bisphosphate (PIP2) by FAK can induce major conformational changes of FAK and exposure of its auto-phosphorylation site, but it cannot induce FAK's activation. Our results support the biological experimental data by providing an atomic description of FAK's conformational changes within FERM and kinase domains.

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