Structural characterization of a novel Cbl phosphotyrosine recognition motif in the APS family of adapter proteins.

@article{Hu2005StructuralCO,
  title={Structural characterization of a novel Cbl phosphotyrosine recognition motif in the APS family of adapter proteins.},
  author={Junjie Hu and Stevan R Hubbard},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 19},
  pages={18943-9}
}
The Cbl adapter proteins typically function to down-regulate activated protein tyrosine kinases and other signaling proteins by coupling them to the ubiquitination machinery for degradation by the proteasome. Cbl proteins bind to specific tyrosine-phosphorylated sequences in target proteins via the tyrosine kinase-binding (TKB) domain, which comprises a four-helix bundle, an EF-hand calcium-binding domain, and a non-conventional Src homology-2 domain. The previously derived consensus sequence… CONTINUE READING