Molecular dynamics characterization of the C2 domain of protein kinase Cbeta.

@article{Banci2002MolecularDC,
  title={Molecular dynamics characterization of the C2 domain of protein kinase Cbeta.},
  author={Lucia Banci and Gabriele Cavallaro and Viktoria Kheifets and Daria Mochly-Rosen},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 15},
  pages={12988-97}
}
Protein kinase C (PKC) isozymes comprise a family of related enzymes that play a central role in many intracellular eukaryotic signaling events. Isozyme specificity is mediated by association of each PKC isozyme with specific anchoring proteins, termed RACKs. The C2 domain of betaPKC contains at least part of the RACK-binding sites. Because the C2 domain contains also a RACK-like sequence (termed pseudo-RACK), it was proposed that this pseudo-RACK site mediates intramolecular interaction with… CONTINUE READING
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