Structure determination and ligand interactions of the PDZ2b domain of PTP-Bas (hPTP1E): splicing-induced modulation of ligand specificity.

@article{Kachel2003StructureDA,
  title={Structure determination and ligand interactions of the PDZ2b domain of PTP-Bas (hPTP1E): splicing-induced modulation of ligand specificity.},
  author={Norman Kachel and Kai Sven Erdmann and Werner Kremer and Peter Wolff and Wolfram Gronwald and Rolf Heumann and Hans Robert Kalbitzer},
  journal={Journal of molecular biology},
  year={2003},
  volume={334 1},
  pages={143-55}
}
Two versions of the PDZ2 domain of the protein tyrosine phosphatase PTP-Bas/human PTP-BL are generated by alternative splicing. The domains differ by the insertion of five amino acid residues and their affinity to the tumour suppressor protein APC. Whereas PDZ2a is able to bind APC in the nanomolar range, PDZ2b shows no apparent interaction with APC. Here the solution structure of the splicing variant of PDZ2 with the insertion has been determined using 2D and 3D heteronuclear NMR experiments… CONTINUE READING

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