Solution structure of the PDZ2 domain from cytosolic human phosphatase hPTP1E complexed with a peptide reveals contribution of the beta2-beta3 loop to PDZ domain-ligand interactions

J Mol Biol. 2002 Jul 19;320(4):813-20. doi: 10.1016/s0022-2836(02)00544-2.

Abstract

The solution structure of the second PDZ domain from human phosphatase hPTP1E in complex with a C-terminal peptide from the guanine nucleotide exchange factor RA-GEF-2 has been determined using 2D and 3D heteronuclear NMR experiments. Compared to previously solved structures, the hPTP1E complex shows an enlarged interaction surface with the C terminus of the bound peptide. Novel contacts were found between the long structured beta2/beta3 loop of the PDZ domain and the sixth amino acid residue from the C terminus of the peptide. This work underlines the importance of the beta2/beta3 loop for ligand selection by PDZ domains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Carrier Proteins / chemistry*
  • Cytosol
  • Guanine Nucleotide Exchange Factors / chemistry*
  • Humans
  • Hydrogen Bonding
  • Ligands
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptides / chemistry
  • Protein Structure, Tertiary
  • Protein Tyrosine Phosphatase, Non-Receptor Type 13
  • Protein Tyrosine Phosphatases / chemistry*
  • Sequence Homology, Amino Acid
  • Solutions

Substances

  • Carrier Proteins
  • Guanine Nucleotide Exchange Factors
  • Ligands
  • Peptides
  • RAPGEF6 protein, human
  • Solutions
  • PTPN13 protein, human
  • Protein Tyrosine Phosphatase, Non-Receptor Type 13
  • Protein Tyrosine Phosphatases

Associated data

  • PDB/1D5G