Efficient T-cell receptor signaling requires a high-affinity interaction between the Gads C-SH3 domain and the SLP-76 RxxK motif.

@article{Seet2007EfficientTR,
  title={Efficient T-cell receptor signaling requires a high-affinity interaction between the Gads C-SH3 domain and the SLP-76 RxxK motif.},
  author={Bruce T. Seet and Donna M. Berry and Jonathan Scott Maltzman and Jacob E Shabason and Monica Raina and Gary A Koretzky and C. Jane McGlade and Tony J. Pawson},
  journal={The EMBO journal},
  year={2007},
  volume={26 3},
  pages={678-89}
}
The relationship between the binding affinity and specificity of modular interaction domains is potentially important in determining biological signaling responses. In signaling from the T-cell receptor (TCR), the Gads C-terminal SH3 domain binds a core RxxK sequence motif in the SLP-76 scaffold. We show that residues surrounding this motif are largely optimized for binding the Gads C-SH3 domain resulting in a high-affinity interaction (K(D)=8-20 nM) that is essential for efficient TCR… CONTINUE READING

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