Single-amino acid substitutions alter the specificity and affinity of PDZ domains for their ligands.

@article{Gee2000SingleaminoAS,
  title={Single-amino acid substitutions alter the specificity and affinity of PDZ domains for their ligands.},
  author={Stephen H. Gee and Simon Quenneville and Christian R. Lombardo and Jos{\'e}e Chabot},
  journal={Biochemistry},
  year={2000},
  volume={39 47},
  pages={14638-46}
}
PDZ domains are modular protein-protein interaction domains that bind to specific C-terminal sequences of membrane proteins and/or to other PDZ domains. Certain PDZ domains in PSD-95 and syntrophins interact with C-terminal peptide ligands and heterodimerize with the extended nNOS PDZ domain. The capacity to interact with nNOS correlates with the presence of a Lys residue in the carboxylate- binding loop of these PDZ domains. Here, we report that substitution of an Arg for Lys-165 in PSD-95… CONTINUE READING