The structural flexibility of the shank1 PDZ domain is important for its binding to different ligands.

@article{Lee2011TheSF,
  title={The structural flexibility of the shank1 PDZ domain is important for its binding to different ligands.},
  author={Jun Hyuck Lee and HaJeung Park and Soo Jeong Park and Hak Jun Kim and Soo Hyun Eom},
  journal={Biochemical and biophysical research communications},
  year={2011},
  volume={407 1},
  pages={207-12}
}
The PDZ domain of the shank protein interacts with numerous cell membrane receptors and cytosolic proteins via the loosely defined binding motif X-(Ser/Thr)-X-Φ-COOH (Φ represents hydrophobic residues) at the carboxyl terminus of its target protein. This enables shank to serve as a membrane-associated scaffold for the assembly of signaling complexes. As the list of proteins that bind to the shank PDZ domain grows, it is not immediately clear what structural element(s) mediate this domain's… CONTINUE READING

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