Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase

@article{Meng1999StructureOT,
  title={Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase},
  author={Wuyi Meng and Sansana Sawasdikosol and Steven J. Burakoff and Michael J. Eck},
  journal={Nature},
  year={1999},
  volume={398},
  pages={84-90}
}
Cbl is an adaptor protein that functions as a negative regulator of many signalling pathways that start from receptors at the cell surface. The evolutionarily conserved amino-terminal region of Cbl (Cbl-N) binds to phosphorylated tyrosine residues and has cell-transforming activity. Point mutations in Cbl that disrupt its recognition of phosphotyrosine also interfere with its negative regulatory function and, in the case of v-cbl, with its oncogenic potential. In T cells, Cbl-N binds to the… 

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