The pseudoactive site of ILK is essential for its binding to alpha-Parvin and localization to focal adhesions.

@article{Fukuda2009ThePS,
  title={The pseudoactive site of ILK is essential for its binding to alpha-Parvin and localization to focal adhesions.},
  author={Koichi Fukuda and Sudhiranjan Gupta and Ka Chen and Chuanyue Wu and Jun Qin},
  journal={Molecular cell},
  year={2009},
  volume={36 5},
  pages={819-30}
}
Integrin-linked kinase (ILK) plays a pivotal role in connecting transmembrane receptor integrin to the actin cytoskeleton and thereby regulating diverse cell-adhesion-dependent processes. The kinase domain (KD) of ILK is indispensable for its function, but the underlying molecular basis remains enigmatic. Here we present the crystal structure of the ILK KD bound to its cytoskeletal regulator, the C-terminal calponin homology domain of alpha-parvin. While maintaining a canonical kinase fold, the… CONTINUE READING
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