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={B. Seet and D. M. Berry and J. Maltzman and J. Shabason and Monica Raina and G. Koretzky and C. McGlade and T. Pawson},
  journal={The EMBO Journal},
  year={2007},
  volume={26}
}
  • B. Seet, D. M. Berry, +5 authors T. Pawson
  • Published 2007
  • Medicine, Biology
  • The EMBO Journal
  • 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 (KD=8–20 nM) that is essential for efficient TCR signaling… CONTINUE READING

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